Recombinant Human Ras Gtpase-Activating Protein 1 (RASA1) Protein (His&Myc)

Name: Recombinant Human Ras Gtpase-Activating Protein 1 (RASA1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-10987P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Ras Gtpase-Activating Protein 1 (RASA1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P20936
Target Symbol	RASA1
Synonyms	CM AVM; CMAVM; DKFZp434N071; GAP; GTPase activating protein; GTPase-activating protein; OTTHUMP00000222390; OTTHUMP00000222391; OTTHUMP00000222392; OTTHUMP00000222393; p120GAP; p120RASGAP; PKWS; Ras GTPase-activating protein 1; RAS p21 protein activator (GTPase activating protein) 1; Ras p21 protein activator; RASA; RASA1; RASA1_HUMAN; RasGAP; Triphosphatase activating protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MEKIMPEEEYSEFKELILQKELHVVYALSHVCGQDRTLLASILLRIFLHEKLESLLLCTLNDREISMEDEATTLFRATTLASTLMEQYMKATATQFVHHALKDSILKIMESKQSCELSPSKLEKNEDVNTNLTHLLNILSELVEKIFMASEILPPTLRYIYGCLQKSVQHKWPTNTTMRTRVVSGFVFLRLICPAILNPRMFNIISDSPSPIAARTLILVAKSVQNLANLVEFGAKEPYMEGVNPFIKSNKHRMIMFLDELGNVPELPDTTEHSRTDLSRDLAALHEICVAHSDELRTLSNERGAQQHVLKKLLAITELLQQKQNQYTKTNDVR
Expression Range	714-1047aa
Protein Length	Partial
Mol. Weight	45.6 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	Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1.
Subcellular Location	Cytoplasm.
Database References	HGNC: 9871 OMIM: 139150 KEGG: hsa:5921 STRING: 9606.ENSP00000274376 UniGene: PMID: 29024832 RASA1 variants are rarely found in children with sporadic capillary malformations of lower limbs without capillary malformation-arteriovenous malformation syndrome. PMID: 29110021 RASA1 mutations are associated melanoma tumorigenesis. PMID: 26993606 MicroRNA-21 reduces RASA1 expression in cervical cancer cell lines and promotes cervical cancer cell migration via RASA1. Furthermore, Ras-induced epithelial-mesenchymal transition contributes to miR-21/RASA1 axis promoting cervical cancer cell migration. PMID: 27101583 These results and the extreme variable expressivity support the hypothesis that somatic "second hits" are required for the development of vascular anomalies associated with CM-AVM syndrome. In addition, the phenotypes of the affected individuals further clarify that lymphatic manifestations are also part of the phenotypic spectrum of RASA1-related disorders. PMID: 26969842 results indicate that, mTOR, Bad, or Survivin are not required for p120 RasGAP fragment N to protect cells from cell death; conclude that downstream targets of Akt other than mTORC1, Bad, or survivin mediate fragment N-induced protection or that several Akt effectors can compensate for each other to induce the pro-survival fragment N-dependent responses PMID: 23826368 The interaction between RASA1 and EPHB4 is an indication of the major cause of capillary malformation with arteriovenous malformation. PMID: 28687708 Low RASA1 expression is associated with Triple-Negative Breast Cancer. PMID: 28108518 QKI-5 stabilized RASA1 mRNA via directly binding to the QKI response element region of RASA1, which in turn prevented the activation of the Ras-MAPK signaling pathway, suppressed cellular proliferation and induced cell cycle arrest. PMID: 27767378 Data show that patients with low level of Ras GTPase-activating protein 1 (RASA1) expression correlated with a significantly poorer survival compared to those with high level of RASA1 expression. PMID: 28179330 Results show that oncogenic KRAS can activate Rho through miR-31-mediated regulation of RASA1 indicating miR-31 acts as a KRAS effector to modulate invasion and migration in pancreatic cancer. PMID: 26747707 Data suggest that, in response to netrin-1/netrin receptor (DCC) signaling, p120RasGAP is recruited to growth cones and supports axon outgrowth; p120RasGAP Src homology 2 domains exhibit scaffolding properties sufficient to support axon outgrowth. PMID: 26710849 Maternal and fetal capillary malformation-arteriovenous malformation due to a novel RASA1 mutation presenting with prenatal non-immune hydrops fetalis have been found. PMID: 26096958 This is the second largest study on isolated, non-syndromic Port-wine stain; data suggest that GNAQ is the main genetic determinant in this condition. Moreover, isolated port-wine stains are distinct from capillary malformations seen in RASA1 disorders. PMID: 26192947 Data showed that hypoxia regulated the expression of miR-182 and RASA1 to promote HCC angiogenesis. PMID: 26126858 p120RasGAP shields Akt from deactivating phosphatases in FGF1 signaling, but loses this ability once cleaved by caspase-3. PMID: 26109071 Capillary malformation-arteriovenous malformation syndrome (CM-AVM) is an autosomal dominant disorder caused by RASA1 mutations. PMID: 25040287 Multifocal, small, round-to-oval, pinkish-to-red cutaneous capillary malformations are seen in more than 90% of people with RASA1 mutations. PMID: 23829194 miR-21 promotes malignant behaviors of colon cancer cells by regulating RASA1 expression via RAS pathways. PMID: 25663768 The individual contribution of each Akt isoform in p120 RasGAP fragment N-mediated cell protection against Fas ligand induced cell death, was investigated. PMID: 25246356 Low RASA1 expression is associated with colorectal cancer. PMID: 25867276 Results show that report that RasGAP associates to PDGFRbeta and prevents its direct activation. This underlying mechanism raises the possibility that PDGFRbeta-mediated diseases involve indirect activation of PDGFRbeta. PMID: 25733681 RASA1 expression is associated with breast cancer progression and poor survival and diseasefree survival of patients. PMID: 25394563 Antisense-mediated knockdown (anti-miR) revealed that miR-206/21 coordinately promote RAS-ERK signaling and the corresponding cell phenotypes by inhibiting translation of the pathway suppressors RASA1 and SPRED1. PMID: 25202123 A ubiquitous binding partner of p190RhoGAP, p120RasGAP (RasGAP), is expressed in much lower levels in DKO4 cells compared to DLD1, and this expression is regulated by KRAS. PMID: 24465899 The results of the present study indicate that P110, in combination with chemotherapeutics, is likely to represent a potential therapeutic strategy for cancer. PMID: 23447049 The novel findings of this study shed light on the molecular mechanisms underlying the DLC1 inhibitory effects of p120 and suggest a functional cross-talk between Ras and Rho proteins at the level of regulatory proteins. PMID: 24443565 RASA1 mutations specifically cause capillary malformation-arteriovenous malformation. PMID: 24038909 These results indicate that stress-activated caspase-3 might contribute to the suppression of metastasis through the generation of fragment N2( RasGAP PMID: 24347041 our study reveals mir-182 suppresses cell proliferation in vivo. RASA1 is related to cell apoptosis. We further show that mir-182 downregulates RASA1 PMID: 24600991 RASA1 mutation is responsible for the aberrant lymphatic architecture and functional abnormalities, as visualized in the PKWS subject and in the animal model. PMID: 23650393 MicroRNA-31 activates the RAS pathway and functions as an oncogenic MicroRNA by repressing RAS p21 GTPase activating protein 1 (RASA1) PMID: 23322774 14-3-3 negatively regulates the RGC downstream of the PI3-kinase/Akt signaling pathway PMID: 23386617 capillary malformation-arteriovenous malformation syndrome; study reports a family with a novel mutation in the RASA1 gene - a truncating mutation in exon 11 of RASA1 (Q503X) PMID: 23158644 Ras and GTPase-activating protein (GAP) drive GTP into a precatalytic state as revealed by combining FTIR and biomolecular simulations PMID: 22949691 multifocal capillary malformations is the key clinical finding to suggest a RASA1 mutation PMID: 22200646 An update of the associated phenotype variability in a family with hereditary capillary malformations caused by a mutation in the RASA1 gene. PMID: 22342634 arguments against G3BP1 being a genuine RasGAP-binding partner PMID: 22205990 Cell adhesion to the substrate is necessary for RasGAP to bind Nck1. Cell detachment makes RasGAP incapable of associating with Nck1 and decreases RasGAP activity. PMID: 21664272 The results assign an unexpected role for p120RasGAP in the regulation of integrin traffic in cancer cells and reveal a new concept of competitive binding of Rab GTPases and GAP proteins to receptors as a regulatory mechanism in trafficking. PMID: 21768288 Nck1 activates RasGAP by direct binding in the substrate-attached but not in the suspended cells. PMID: 21664272 An important role is revealed for p120 RasGAP (RASA1) as a transgenic regulator of CD4+CD8+ double-positive cell survival and positive selection in the thymus as well as naive T cell survival in the periphery. PMID: 21646295 Ras mutation cooperates with beta-catenin activation to drive bladder tumourigenesis. PMID: 21368895 A novel synonymous mutation (c.1229 G > A [p.K420K]) of RASA1 was identified in a Chinese population with sporadic Sturge-Weber syndrome PMID: 20821215 Sema4D/Plexin-B1 promotes the dephosphorylation and activation of PTEN through the R-Ras GAP activity, inducing growth cone collapse. PMID: 20610402 miR-132 acts as an angiogenic switch by suppressing endothelial p120RasGAP expression. PMID: 20676106 In a collaborative study, 5 index patients (2 females, 3 males) with spinal AVMs or AVFs and cutaneous multifocal capillary lesions were investigated for the RASA1 gene mutation. PMID: 20007727 We show a novel alternative pathway of apoptosis in human primary cells that is mediated by transcriptionally dependent decreases in p53 and c-Myc and decreases in p21. PMID: 11751853 N-terminal fragment generated by caspase cleavage protects cells in a Ras/PI3K/Akt-dependent manner that does not rely on NFkappa B activation PMID: 11847220 mutual regulation of Ras and NF1-GAP is essential for normal neuronal differentiation PMID: 12730209

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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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