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Validated All-in-One™ qPCR Primer for GP1BA(NM_000173.6) Search again
Product ID:
HQP099013
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BDPLT1, BDPLT3, BSS, CD42B, CD42b-alpha, DBPLT3, GP1B, GPIbA, GPIbalpha, VWDP
Gene Description:
glycoprotein Ib platelet subunit alpha
Target Gene Accession:
NM_000173.6(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V.
Gene References into function
- The von Willebrand factor- and thrombin-binding activities of recombinant GPIb alpha(1-289) expressed in a baculovirus/insect cell system are identical to those of an equivalent fragment derived from human platelets.
- Both the high affinity thrombin receptor (GPIb-IX-V) and GPIIb/IIIa are implicated in expression of thrombin-induced platelet procoagulant activity.
- Two compound heterozygotes for the GPIbalpha gene(a maternal T insertion at position 1418 causing a translational frameshift and premature polypeptide termination, and a paternal T715A substitution changing Cys209 to Ser)had Bernard-Soulier syndrome.
- GP Ibalpha initiates ERK activation, and regulates ERK-induced EC migration on vWF.
- Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3
- Molecular models of the 7 Leu-rich repeats of human GPIb alpha, illustrate the species-specific interaction between human vWF and its receptor. A large negatively charged patch exists on the concave face of repeats 2-4.
- Platelet glycoprotein Ib function and reactivity of platelets was studied in diabetic and non-diabetic hemodialysed pts. GP1B level and function was decreased only in non-DM pts.
- The Kozak sequence polymorphism of the glycoprotein Ib alpha gene had no impact on the risk of coronary heart disease, its effect on extent of CHD remains to be seen.
- Absence of GPIbalpha is responsible for aberrant membrane development during megakaryocyte maturation; leads to abnormal partitioning of the membrane systems and abnormal proplatelet production.
- Identification of the regulatory elements of the human von Willebrand factor for binding to platelet GPIb
- Anti-vWf antibodies induce GPIbalpha and FcgammaRII mediated platelet aggregation only at low shear forces.
- Site-directed mutagenesis demonstrates residues involved in the sulfation of tyrosines 276, 278, and 279 and residues crucial for botrocetin-mediated VWF binding.
- Hypercholesterolemia primes platelets for recruitment via VWF, GPIb alpha, and P-selectin to lesion-prone sites, before lesions are detectable. Platelet tethering to vascular endothelium was mainly mediated by platelet GPIb alpha
- A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha.
- the rGPIa/IIa-collagen interaction dominates the adhesion of rGPIa/IIa-Ib alpha-liposomes to the collagen surface at low shear rates; the rGPIa/IIa-collagen and rGPIb alpha-VWF interactions synergistically support liposome adhesion at high shear rates.
- crystal structure of N-terminal domain reveals an unmasking mechanism for receptor activation
- A role for glycoprotein Ib in Streptococcus sanguis-induced platelet aggregation.
- structures of the glycoprotein Ibalpha amino-terminal domain and its complex with the Von Willebrand factor domain A1 are presented
- The mucin-like macroglycopeptide region of glycoprotein Ibalpha is required for cell adhesion to immobilized von Willebrand factor (VWF) under flow but not for static VWF binding.
- Ligand binding of GPIb, without receptor clustering, is sufficient to activate Src.
- structure-activity relationship of mutations found in Bernard-Soulier syndrome
- The polymorphisms affecting the structure or level of the main adhesive platelet glycoproteins (GPs) plays a minor role in genetic risk factors for arterial thrombotic disorders.
- A role of the GPIb alpha intracellular domain was shown. VWF-dependent adhesion of cells containing deletions of the entire (Delta 518-610) or portions (Delta 535-568, Delta 569-610) of the GPIb alpha cytoplasmic tail was insensitive to RAM.1 inhibition.
- The cytoplasmic domain of GPIb alpha is important in the GPIb-IX-von Willebrand factor interaction under both static and flow conditions, modulating the strength of the bond between receptor and ligand.
- analysis of kinetic and mechanical properties of tether bonds formed between patient VWD platelets and the A1-domain of VWF indicate that GPIba mutation, Gly233Val, promotes and stabilizes platelet adhesion to VWF
- binding of thrombin to GPIbalpha induces fibrin binding to resting alphaIIbbeta3 leading to fibrin-dependent platelet aggregation and clot retraction, that can be selectively inhibited by alphaIIbbeta3 antagonists
- shear-dependent VWF-induced platelet activation affects filamin A binding to GpIb-IX-V, and filamin A binding to the cytoplasmic tail of GpIbalpha regulates proaggregatory tyrosine kinase signaling.
- determined the structure of platelet glycoprotein Ibalpha (GpIbalpha) bound to thrombin at 2.3 angstrom resolution and defined two sites in GpIbalpha that bind to exosite II and exosite I of two distinct alpha-thrombin molecules, respectively
- crystal structure of the GpIbalpha-thrombin complex at 2.6 angstrom resolution reveals simultaneous interactions of GpIbalpha with exosite I of one thrombin molecule, and with exosite II of a second thrombin molecule
- in human platelets, GPIbalpha and ADP act in synergy to amplify PAR1 coupled responses while PAR4 is activated independently of GPIbalpha and ADP.
- Convulxin binds weakly to murine platelet GPIb alpha but more strongly to human platelet GPIb alpha
- Mac-1 and glycoprotein Ib bind in an interaction mediated by high molecular weight kininogen
- GPIb alpha plays a critical role in the co-localization of thrombin and factor XI and the resultant efficient activation of FXI
- GPIb translocation is powered by a contractile mechanism involving Ca2+ mobilization, actin polymerization, and myosin incorporation into the cytoskeleton and both PAR-1 and PAR-4 can activate this process
- association between the presence of different VNTR alleles of GP Ibalpha and the frequency of coronary heart disease
- The presence of the VNTR B allele of glycoprotein Ibalpha confers a significant risk for NAION (nonarteritic anterior ischemic optic neuropathy)
- binding of thrombin to GPIbalpha induced an intracellular signaling leading to the interaction of the platelet integrin alphaIIbbeta3 with the fibrin-dodecapeptide sequence of the gamma chain
- in the absence of GPIbalpha or following inhibition of thrombin binding to GPIbalpha, there is a reduction in the thrombin-induced calcium flux, beta3 cleavage and micro -calpain activation.
- existence of a second major 14-3-3zeta binding site within the cytoplasmic tail of GPIbalpha that has an important functional role in regulating integrin-dependent cell spreading.
- Results suggest that von Willebrand factor domain A1 inhibits the cleavage of domain A2 by ADAMTS13, and that inhibition can be relieved by interaction of domain A1 with platelet platelet glycoprotein Ibalpha or certain glycosaminoglycans.
- VNTR of the GPIba gene may have a role in development of myocardial infarction
- The homozygous glycoprotein 1b alpha (-5)T/C Kozak polymorphism increases the risk of ischemic cerebrovascular events 3.5 fold, consistent with its reported gene dose effect on GP 1b alpha/IX/V receptor density on platelets.
- binding of FXI to GPIbalpha is mediated by amino acids in the A3 domain in the presence or absence of HK.
- AP1 protein binds to specific region, which facilitates binding to Von Willebrand factor.
- FXI binds to glycoprotein Ibalpha at sites comprising the leucine-rich repeat sequences within the NH2-terminal globular domain that are separate and distinct from the thrombin-binding site
- Streptoccus gordonii Gspb and Hsa mediate streptococcal adherence to sialylated platelet membrane glycoprotein Ibalpha
- the association involves an interaction between the ectodomains of GPIb alpha and GPVI
- a gain-of-function phenotype resulting from mutations in the LRR region of GP Ibalpha; data suggest that the LRRs regulate GP Ibalpha affinity for VWF allosterically
- analysis of platelet glycoprotein I(b)alpha and integrin alpha2beta1 polymorphisms in diverse populations
- GPIbalpha and GPV are shed through an ADAM17-dependent mechanism after aspirin administration
- GP Ibalpha is a physiologically relevant ligand for alphaMbeta2 and that integrin engagement of GP Ibalpha is critical to leukocyte function and the biological response to vascular injury.
- domain translocation in VWF allows interaction with GPIbalpha
- An SIV vector carrying human factorVIII (hFVIII) driven by the GPIbalpha promoter induced production of transcripts of the hFVIII gene and the hFVIII antigen in bone marrow and spleen for production of detectable transcripts of the hFVIII gene.
- Data demonstrate that LRR2-4, encompassing a pronounced negative charge patch on human glycoprotein (GP)Ibalpha, is essential for GPIbalpha.von Willebrand factor-dependent adhesion as hydrodynamic shear increases.
- The -5T/C polymorphism of the platelet glycoprotein GPIb alpha Kozak gene is implicated in the pathogenesis of transient ischemic attack. C allele is an independent risk factor for TIA.
- A novel mutation, Trp207Gly, causes BSS and predicts disruption of the interaction between a disulfide loop and the LRR domain that is essential for the integrity of GPIbalpha structure
- platelets adhere to dimeric beta2GPI under both arterial and venous shear stresses. Platelets adhere via two receptors: GPIbalpha and apoER2'. These receptors are present in a complex on the platelet surface
- Functional role of the 557-569 domain of GPIbalpha in controlling von Willebrand factor-dependent adhesion and signaling in platelets.
- genotyped 2090 women in Heart and Estrogen/progestin Replacement Study for functional polymorphisms in GP1BA and GP6 and assessed the coronary heart disease
- Our results indicate that the platelet glycoprotein Ib-alpha polymorphisms are not associated with an increased risk for AMI at early onset (< 46 years) both in men and in women.
- T145M polymorphism of the GPIbalpha subunit predicts risk for recurrent coronary events in diabetic postinfarction patients.
- Using a 328-base-pair fragment of the human GpIbalpha gene regulatory sequence, in the context of a lentiviral vector, tightly restricts transgene expression to the megakaryocytic lineage after transduction of human CD34(+) hematopoietic cells.
- both the gpIb-VWF interaction and the integrin alpha(2)beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II)beta(1) makes a greater contribution to adhesion to type I collagen because less VWF is bound
- REVIEW: The platelet adhesion receptor, the glycoprotein Ib-IX-V complex, not only mediates platelet adhesion but also transmits signals leading to platelet activation, aggregation and secretion
- support the hypothesis that platelet GP Ib-IX functions that support normal hemostasis or pathologic thrombosis also contribute to tumor malignancy
- REVIEW OF GP1BB AND GP1BA BINDING SITES FOR LIGANDS, INTERACTIONS WITH VWF AND THROMBIN, ROLE IN PLATELET ACTIVATION
- VWF A/T1381 polymorphism plays an important role in inter-individual variability of the affinity of VWF for GPIbalpha, with T/T variants having a higher affinity than A/A and A/T variants
- The BC genotype of the VNTR polymorphism of GPIb-alpha is an independent predictor of recurrent events in stroke patients treated with aspirin.
- Platelets polymorphisms may contribute to the risk of TE, mainly those of glycoprotein (GP)Ibalpha.
- 3 families from Iran with Bernard-Soulier syndrome were investigated; the presence of the same GpIX Phe55Ser missense mutation in two families and of a single base insertion (GP1BA C3221 ins) in the third family were demonstrated
- Increased expression of Glycoprotein Ib alpha is associated with cancer
- The transmembrane domain of GPIX plays an important role in expression and assembly of the GPIb-IX complex by interacting with its counterparts of GPIb.
- thrombin mutant WE (Trp215Ala and Glu217Ala), while not activating platelets, retains the ability to interact with platelets through GPIb (glycoprotein Ib (platelet) alpha); inhibits GPIb-dependent binding to von Willebrand factor-collagen under shear.
- Polymorphisms in human platelet alloantigen (HPA)-1 and HPA-3 (GPIIb/IIIa), HPA-2 (GPIb/IX), HPA-4 (GPIIIa) and HPA-5 (GPIa/IIa) were found to be associated with the symptoms and recurrence of ischemic stroke.
- the VNTR polymorphism of the GPIbalpha gene, which affects the structure and function of this platelet glycoprotein, seems to be associated with risk for oral cancer, especially in patients without a family history of cancer
- GPIbalpha residue Tyr276 is physiologically important, supporting stable thrombus formation in vivo.
- laminin supports platelet adhesion depending on the interaction of VWF and GPIb-IX-V under pathophysiological high shear flow
- protein C and APC may directly promote cell signaling in other cells by binding to ApoER2 and/or GPIbalpha
- important role for Lyn in VWF/GPIb-IX-induced integrin activation mediated via the cGMP signaling pathway independently of TXA2 synthesis and also indicate that Lyn is critically important in GPIb-IX-mediated activation of the cGMP pathway
- glycoprotein Ib-IX-V complex contributes to tissue factor-independent thrombin generation by recombinant factor VIIa on the activated platelet surface
- Data demonstrate the native-like heteromeric interaction among the isolated Ibalpha, Ib beta and IX TM peptides, which provides support for the four-helix bundle model of the TM domains in the glycoprotein Ib-IX complex.
- in type 2B vWD, prolonged lifetimes of vWF bonds with GPIbalpha on circulating platelets may allow ADAMTS-13 to deplete large vWF multimers, causing bleeding
- 3 members of a family were found to have a TGAG deletion starting from the last base of the codon for Ser39, leading to a coding frame shift with a new termination codon after 11 novel amino acids.
- Sequencing analysis of the GPIbalpha gene revealed a novel heterozygous mutation, A169C, resulting in an N41H substitution in the protein in Bernard-Soulier syndrome.
- role of filamin cleavage and protein tyrosine phosphorylation in shear-stress-induced platelet microparticle formation, and of its suppression by the monoclonal antibody (mAb) Ib-23 directed against GPIbalpha
- the domains of GpIbalpha mediating c-Myc-like functions are modular, genetically distinct, and independent of those involved in vWFR signaling.
- The changes in amino-acids expression induced by the two loci brought no significant influence on GP I b and GP II b- III a activities.