Recombinant Human Plexin-B1 (PLXNB1) Protein (His&Myc)

Name: Recombinant Human Plexin-B1 (PLXNB1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06589P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Plexin-B1 (PLXNB1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O43157
Target Symbol	PLXNB1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	LQHLARDPTSGTLYLGATNFLFQLSPGLQLEATVSTGPVLDSRDCLPPVMPDECPQAQPTNNPNQLLLVSPGALVVCGSVHQGVCEQRRLGQLEQLLLRPERPGDTQYVAANDPAV
Expression Range	35-150aa
Protein Length	Partial
Mol. Weight	19.9 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Receptor for SEMA4D. Plays a role in GABAergic synapse development. Mediates SEMA4A- and SEMA4D-dependent inhibitory synapse development. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration.
Subcellular Location	[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.; [Isoform 3]: Secreted.
Protein Families	Plexin family
Database References	HGNC: 9103 OMIM: 601053 KEGG: hsa:5364 STRING: 9606.ENSP00000296440 UniGene: PMID: 29040270 The positive expression of both Sema4D and PlexinB1 was found to be an independent risk factor for a worse survival in colorectal cancer. PMID: 27456345 Loss of plexin B1 expression might play a pivotal role in enhancing the metastatic potential of breast cancer cells. PMID: 28739743 Plexin B1 expression was regulated by TMPRSS2-ERG fusion gene in prostate cancer. PMID: 28004109 Plexin-B1 mediates RhoA/integrin alphavbeta3 involved in the PI3K/Akt pathway and SRPK1 to influence the growth of glioma cell, angiogenesis, and motility in vitro and in vivo. PMID: 26944058 results show that Sema4D/plexin-B1 signaling promotes the translocation of androgen receptor to the nucleus and thereby enhances AR transcriptional activity PMID: 25982277 Plexin-B1 induces cutaneous squamous cell carcinoma cell proliferation, migration, and invasion by interacting with Sema4D. Plexin-B1 might serve as a useful biomarker and/or as a novel therapeutic target for cSCC. PMID: 26051877 Results show that decreased expression of Sema4D, plexin-B1 and -B2 was associated with local recurrence and poor prognosis of breast neoplasm. PMID: 26035216 Dysregulation of the vascular endothelial growth factor and semaphorin ligand-receptor families in prostate cancer metastasis PMID: 26341082 Blocking of CD100, plexin B1 and/or B2 in adhesion experiments have shown that both CD100 and plexins act as adhesion molecules involved in monocyte-endothelial cell binding. PMID: 26275342 Activation of endogenous plexin-B1 enhances cell migration and tumor invasiveness in prostate cancer cells. PMID: 23775445 Data indicate that Rnd1 efficiently displaces Rac1 from its complex with Plexin-B1 but not vice versa. PMID: 23603360 ErbB-2 overexpression in human breast & ovarian cancer cell lines leads to phosphorylation & activation of Plexin-B1. This was required for ErbB-2-dependent activation of RhoA & RhoC & promoted invasive behavior. PMID: 22378040 PlexinB1 mutations block plexinB1-mediated signalling pathways that inhibit cell motility. PMID: 22404908 evidence that Sema4D/Plexin-B1-mediated NF-kappaB activation and IL-8 production is critical in the generation a pro-angiogenic phenotype in endothelial cells PMID: 22028792 Two crystal structures of the human Plexin-B1 cytoplasmic region in complex with a constitutively active RhoGTPase, Rac1, are reported. PMID: 21912513 The binding of Sema4D to plexinB1 induced small GTPase Ras homolog gene family, member A activation and resulted in the phosphorylation of MAPK and Akt. PMID: 21812859 plexin-B1, a target of miR-214, may function as an oncogene in human cervical cancer HeLa cells PMID: 21216304 Plexin B1 abrogates integrin-dependent migration and activation of pp125(FAK). PMID: 21029396 Plexin-B1 expression correlates with malignant phenotypes of serous ovarian tumors, probably via phosphorylation of AKT at Ser473 PMID: 21059203 crystal structures of cognate complexes of the semaphorin-binding regions of plexins B1 and A2 with semaphorin ectodomains (human PLXNB1(1-2)-SEMA4D(ecto) and murine PlxnA2(1-4)-Sema6A(ecto)), plus unliganded structures of PlxnA2(1-4) and Sema6A(ecto) PMID: 20877282 Sema4D/Plexin-B1 promotes the dephosphorylation and activation of PTEN through the R-Ras GAP activity, inducing growth cone collapse. PMID: 20610402 Plexin B1 may function as a tumor promoter in melanomas not driven by c-Met activation. PMID: 20164843 Data show that Plex-B1 assumes a predictive value for unfavourable outcome when co-expressed with Met. PMID: 19940359 The plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding PMID: 11937491 LARG plays a critical role in plexin-B1 signaling to stimulate Rho activation and cytoskeletal reorganization. PMID: 12196628 Interaction of plexin-B1 with PDZ domain-containing Rho guanine nucleotide exchange factors PMID: 12220504 Plexin-B1 is an easily accessible receptor for CD100 within the immune system. The crosstalk operated by the CD100/Plexin-B1 interaction is not malignancy related but reproduces a mechanism used by normal CD5+ B cells. PMID: 12406905 cleavage by proprotein convertases is a novel regulatory step for semaphorin receptors localized at the cell surface. PMID: 12533544 In some human neoplastic lines, PLXB1 is overexpressed, constitutively tyrosine phosphorylated, and associated with Scatter Factor Receptors. PMID: 15184888 ErbB-2-mediated phosphorylation of plexin-B1 is critically involved in Sema4D-induced RhoA activation. PMID: 15210733 demonstrate that Sema4D is angiogenic in vitro and in vivo and that this effect is mediated by its high-affinity receptor, Plexin B1, and that biologic effects elicited by Plexin B1 require coupling and activation of the Met tyrosine kinase PMID: 15632204 the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold, as shown by NMR PMID: 15929008 Semaphorin 4D/plexin-B1 induces endothelial cell migration through the activation of PYK2, Src, and the phosphatidylinositol 3-kinase-Akt pathway PMID: 16055703 Plexin-B1 contributes to trophoblast-endometrium interactions, most likely by enhancing adhesion properties. PMID: 17383649 Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain PMID: 17916560 13 somatic missense mutations in the cytoplasmic domain of the Plexin-B1 gene hinder Rac & R-Ras binding & R-RasGAP activity, & increase cell motility, invasion, adhesion, & lamellipodia extension. PMID: 18024597 a novel mechanism by which plexin-mediated signaling can be regulated and explains how Sema4D can exert different biological activities through the differential association of its receptor with ErbB-2 and Met. PMID: 18025083 NMR solution structure of the Rho GTPase binding domain; study suggests that the oncogenic behavior of the mutants can be rationalized with reference to the structure of the RBD of plexin-B1 PMID: 18275816 Plexin B1 protein is absent in more than 80% of renal cell carcinomas. when we have induced plexin B1 expression with an expression vector in the renal adenocarcinoma cell line ACHN, a marked reduction in proliferation rate was produced. PMID: 18279812 Mapping of the Rac1 GTPase surface that contacts the Rho GTPase binding domain of plexin-B1 by NMR confirms the plexin domain as a GTPase effector protein and regions neighboring the GTPase switch I and II regions are also involved in the interaction. PMID: 18321527 Plexin B1 expression is reduced in the group of "uncoupled" stem cell-like breast cancer tumors PMID: 18417270 Plexin-B1 is a dual functional GTPase activating protein for R-Ras and M-Ras, remodelling axon and dendrite morphology, respectively. PMID: 19444311 B-Raf/MKK/ERK provides a permissive environment for melanoma genesis by modulating plexin B1. PMID: 19483722 show here that activation of plexin-B1 by Semaphorin 4D and its subsequent tyrosine phosphorylation creates docking sites for the SH2 domains of phospholipase Cgamma. PMID: 19805522 the monomeric intracellular plexin-B1 binds R-Ras but not H-Ras. These findings suggest that the monomeric form of the intracellular region is primed for GAP activity and extend a model for plexin activation. PMID: 19843518

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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