Search results
1000 results found for “Creatine Kinases”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
CST3 Mouse, ActiveDescription:
Cystatin-C Mouse Recombinant, Active
Cystatin-C, Cystatin-3, Cst3, CST3
Product # :
PRO-2433Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.
More Info
-
Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
-
Synonyms
Cystatin-C, Cystatin-3, Cst3, CST3
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HCST HumanDescription:
Hematopoietic Cell Signal Transducer Human Recombinant
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
Product # :
PRO-2522Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HCST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 271 amino acids (20-48 a.a.) and having a molecular mass of 30.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).HCST is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HCST protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
HCST (Hematopoietic Cell Signal Transducer) is part of the DAP10 family. HCST is capable of being a part of an immunoreceptor complex. HCST takes a vital part in inducing cytotoxicity against MHC class I chain-associated MICA & target cells expressing cell surface ligands such as UL16-binding protein (ULBP) & MICB. HCST complex participates in proliferation as well as cell survival by activating T & NK cell responses.
-
Synonyms
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPTTPGERS SLPAFYPGTS GSCSGCGSLS LPLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGFR Human Sf9, ActiveDescription:
Epidermal Growth Factor Receptor Human Recombinant Sf9, Active
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Product # :
PKA-335Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- biological activity
- More Info
Description
EGFR Human Recombinant encoding a.a. 672-1210 expressed in Baculovirus infected Sf9 cells, fused with a GST-tag at N-terminus with thrombin cleavage sites, having a molecular weight of 89,171 Dalton.EGFR is purified by proprietary chromatographic techniques.
Source
Baculovirus infected Sf9 cells.
Formulation
EGFR in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT, 15mM reduced glutathione and 20% glycerol.
Biological Activity
Determination of Km value by Filter binding assay MAFC membrane.
More Info
-
Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
-
Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
-
Physical Appearance
Sterile filtered liquid.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please avoid freeze-thaw cycles.
-
Specific Activity
30 pmol/µgxmin.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Ang K1-3 HumanDescription:
Angiostatin Kringles 1-3 Human Recombinant
Angiostatin, Angiostatin Kringles 1-3, Ang K1-3.
Product # :
PRO-284Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Angiostatin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids and having a molecular mass of approximately 29.7 kDa. The Ang K1-3 is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM NaAc, pH5.5, 4% mannitol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is assayed on anti-proliferation and anti-migration of endothelial cells in vitro and anti-angiogenesis in vivo. The specific activity of anti-migration of endothelial cells in vitro is 550,000 Units/mg.
More Info
-
Introduction
Ang K1-3 is a proteolytic fragment of plasminogen containing the first three kringle structures. A specific inhibitor of endothelial cell growth and angiogenesis. More active relative to kringles 1-4. Ang K1-3 reduces endothelial cell proliferation and acts as a potent inhibitor of angiogenesis and tumor growth.
-
Synonyms
Angiostatin, Angiostatin Kringles 1-3, Ang K1-3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
The lyophilized Angiostatin K1-3 is stable for several weeks at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
-
Solubility
We recommend to briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
-
Amino Acid Sequence
VYLSECKTGN GKNYRGTMSK TKNGITCQKW SSTSPHRPRF SPATHPSEGL EENYCRNPDN DPQGPWCYTT DPEKRYDYCD ILECEEECMH CSGENYDGKI SKTMSGLECQ AWDSQSPHAH GYIPSKFPNK NLKKNYCRNP DRELRPWCFT TDPNKRWELC DIPRCTTPPP SSGPTYQCLKGTGENYRGNV AVTVSGHTCQ HWSAQTPHTH NRTPENFPCK NLDENYCRNP DGKRAPWCHT TNSQVRWEYC KIPSCDSSP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CDO1 HumanDescription:
Cysteine Dioxygenase Human Recombinant
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
Product # :
ENZ-449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.The CDO1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDO1 solution contains 20mM Tris buffer(pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.
-
Synonyms
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CNRIP1 HumanDescription:
Cannabinoid Receptor Interacting Protein 1 Human Recombinant
Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.
Product # :
PRO-1214Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNRIP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 187 amino acids (1-164) and having a molecular mass of 21.0 kDa.CNRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CNRIP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.
-
Synonyms
Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGDLPGL VRLSIALRIQ PNDGPVFYKV DGQRFGQNRT IKLLTGSSYK VEVKIKPSTL QVENISIGGV LVPLELKSKE PDGDRVVYTG TYDTEGVTPT KSGERQPIQI TMPFTDIGTF ETVWQVKFYN YHKRDHCQWG SPFSVIEYEC KPNETRSLMW VNKESFL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SNTA1 HumanDescription:
Syntrophin, Alpha 1 Human Recombinant
Alpha-1-syntrophin, 59 kDa dystrophin-associated protein A1 acidic component 1, Pro-TGF-alpha cytoplasmic domain-interacting protein 1, TACIP1, Syntrophin-1, SNTA1, SNT1, LQT12, dJ1187J4.5.
Product # :
PRO-1016Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (1-505 a.a.) and having a molecular mass of 56.3kDa. SNTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SNTA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
SNTA1 is a member of the syntrophin gene family. SNTA1 is a peripheral membrane protein found linked with dystrophin and dystrophin-related proteins. Dystrophin is a large, rod-like cytoskeletal protein located at the inner surface of muscle fibers. Dystrophin is absent in Duchenne Muscular Dystrophy patients, however it is present in reduced amounts in Becker Muscular Dystrophy patients. Syntrophins are cytoplasmic peripheral membrane scaffold proteins and components of the dystrophin-associated protein complex. The N-terminal PDZ domain of SNTA1 interacts with the C-terminus of the pore-forming alpha subunit (SCN5A) of the cardiac sodium channel Nav1.5. In addition, SNTA1 associates cardiac sodium channels with the nitric oxide synthase-PMCA4b (plasma membrane Ca-ATPase subtype 4b) complex in cardiomyocytes. The SNTA1 gene is a predisposition locus for Long-QT syndrome (LQT) - an inherited disorder associated with sudden cardiac death from arrhythmia - and sudden infant death syndrome (SIDS). SNTA1 also associates with dystrophin and dystrophin-related proteins at the neuromuscular junction and modifies intracellular calcium ion levels in muscle tissue.
-
Synonyms
Alpha-1-syntrophin, 59 kDa dystrophin-associated protein A1 acidic component 1, Pro-TGF-alpha cytoplasmic domain-interacting protein 1, TACIP1, Syntrophin-1, SNTA1, SNT1, LQT12, dJ1187J4.5.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASGRRA PRTGLLELRA GAGSGAGGER WQRVLLSLAE DVLTVSPADG DPGPEPGAPR EQEPAQLNGA AEPGAGPPQL PEALLLQRRR VTVRKADAGG LGISIKGGRE NKMPILISKI FKGLAADQTE ALFVGDAILS VNGEDLSSAT HDEAVQVLKK TGKEVVLEVK YMKDVSPYFK NSTGGTSVGW DSPPASPLQR QPSSPGPTPR NFSEAKHMSL KMAYVSKRCT PNDPEPRYLE ICSADGQDTL FLRAKDEASA RSWATAIQAQ VNTLTPRVKD ELQALLAATS TAGSQDIKQI GWLTEQLPSG GTAPTLALLT EKELLLYLSL PETREALSRP ARTAPLIATR LVHSGPSKGS VPYDAELSFA LRTGTRHGVD THLFSVESPQ ELAAWTRQLV DGCHRAAEGV QEVSTACTWN GRPCSLSVHI DKGFTLWAAE PGAARAVLLR QPFEKLQMSS DDGASLLFLD FGGAEGEIQL DLHSCPKTIV FIIHSFLSAK VTRLGLLA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SOST Human, HEKDescription:
Sclerostin Human Recombinant, HEK
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-2481Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).
Source
HEK293 Cells.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
-
Synonyms
Sclerostin, SOST, CDD, VBCH.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BCAR1 HumanDescription:
Breast Cancer Anti-Estrogen Resistance 1 Human Recombinant
CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.
Product # :
PRO-1858Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BCAR1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 407 amino acids (465-848) and having a molecular mass of 43.9kDa. BCAR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCAR1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Breast Cancer Anti-Estrogen Resistance 1 (BCAR1) is a Src family kinase substrate which takes part in a range of cellular events such as migration, survival, transformation, and invasion. BCAR1 plays a vital role for tyrosine kinase-based signaling related to cell adhesion.
-
Synonyms
CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRLQQGVS ATVAHLLDLA GSAGATGSWR SPSEPQEPLV QDLQAAVAAV QSAVHELLEF ARSAVGNAAH TSDRALHAKL SRQLQKMEDV HQTLVAHGQA LDAGRGGSGA TLEDLDRLVA CSRAVPEDAK QLASFLHGNA SLLFRRTKAT APGPEGGGTL HPNPTDKTSS IQSRPLPSPP KFTSQDSPDG QYENSEGGWM EDYDYVHLQG KEEFEKTQKE LLEKGSITRQ GKSQLELQQL KQFERLEQEV SRPIDHDLAN WTPAQPLAPG RTGGLGPSDR QLLLFYLEQC EANLTTLTNA VDAFFTAVAT NQPPKIFVAH SKFVILSAHK LVFIGDTLSR QAKAADVRSQ VTHYSNLLCD LLRGIVATTK AAALQYPSPS AAQDMVE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FARS2 HumanDescription:
Phenylalanyl-tRNA Synthetase 2 Human Recombinant
Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.
Product # :
ENZ-111Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FARS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (37-451 a.a.) and having a molecular mass of 50.6kDa.FARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FARS2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.
-
Synonyms
Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPAAECATQR APGSVVELLG KSYPQDDHSN LTRKVLTRVG RNLHNQQHHP LWLIKERVKE HFYKQYVGRF GTPLFSVYDN LSPVVTTWQN FDSLLIPADH PSRKKGDNYY LNRTHMLRAH TSAHQWDLLH AGLDAFLVVG DVYRRDQIDS QHYPIFHQLE AVRLFSKHEL FAGIKDGESL QLFEQSSRSA HKQETHTMEA VKLVEFDLKQ TLTRLMAHLF GDELEIRWVD CYFPFTHPSF EMEINFHGEW LEVLGCGVME QQLVNSAGAQ DRIGWAFGLG LERLAMILYD IPDIRLFWCE DERFLKQFCV SNINQKVKFQ PLSKYPAVIN DISFWLPSEN YAENDFYDLV RTIGGDLVEK VDLIDKFVHP KTHKTSHCYR ITYRHMERTL SQREVRHIHQ ALQEAAVQLL GVEGRF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CST3 Protein, HisDescription:
Cystatin-C Human Recombinant, His Tag
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-656Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
-
Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
-
Synonyms
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AKR1B1 HumanDescription:
Aldose Reductase Human Recombinant
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
Product # :
ENZ-390Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
AKR1B1 Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids having a molecular mass of 35.8 kDa.The AKR1B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 1mg/ml protein solution contains 20mM Tris-HCl buffer pH 8, 10% glycerol, and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 800pmol/min/ug, and is defined as the amount of enzyme that catalyze the reduction of 1.0 pmole DL-glyceraldehyde in the presence of NADPH per minute at pH7.0 at 37°C.More Info
-
Introduction
AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.
-
Synonyms
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA LLSCTSHKDY PFHEEF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
-
Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SNCA MouseDescription:
Alpha-Synuclein Mouse Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, α-Synuclein, SNCA, Syn, SNCA.
Product # :
PRO-858Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNCA Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 14.4 kDa. The SNCA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA protein contains 20mM Tris-HCl buffer (pH 7.5) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
-
Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, α-Synuclein, SNCA, Syn, SNCA.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP GSEAYEMPSE EGYQDYEPEA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NMT2 HumanDescription:
N-Myristoyltransferase 2 Human Recombinant
Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.
Product # :
ENZ-068Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NMT2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 518 amino acids (1-498 a.a.) and having a molecular mass of 59.1kDa. The NMT2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NMT2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glycylpeptide N-tetradecan-oyltransferases 2 (NMT2) is a cytoplasmic protein which is a member of the NMT family of proteins. The proteins in the NMT family catalyze the addition of a myristoyl group to the N-terminal glycine residue of eukaryotic, fungal and viral proteins. These proteins are mostly detected in the heart, gut, kidney, liver and placenta. NMT catalyzes the reaction of N-terminal myristoylation of various signaling proteins. NMT transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. There are several distinct NMTs which vary in the molecular weight and /or subcellular distribution.
-
Synonyms
Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK KQKRKKEKPN SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ FWDTQPVPKL DEVITSHGAI EPDKDNVRQE PYSLPQGFMW DTLDLSDAEV LKELYTLLNE NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH RSLNPKKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS VRELINTYLK QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL SFYTLPSTVM HHPAHKSLKA AYSFYNIHTE TPLLDLMSDA LILAKSKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL YNWRCPGTDS EKVGLVLQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EG VEGF HumanDescription:
Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant
PK1, PRK1, Prokineticin 1, EG-VEGF.
Product # :
CYT-338Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
More Info
-
Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
-
Synonyms
PK1, PRK1, Prokineticin 1, EG-VEGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
-
Background
Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications
Abstract:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.Introduction:
Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.Production and Characterization:
Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.Role in Endocrine Disorders:
EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.Therapeutic Implications:
Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.Conclusion:
Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.7kDa.
What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.
What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EG-VEGF Protein?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.
What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SUMO3 HumanDescription:
Small Ubiquitin-Related Modifier 3 Human Recombinant
SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.
Product # :
PRO-267Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SUMO3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Nevertheless, unlike ubiquitin that targets proteins for degradation, SUMO3 protein takes part in several cellular processes, like nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO3 regulates amyloid beta generation and is crucial in the onset or progression of Alzheimer’s disease.
-
Synonyms
SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PCNP HumanDescription:
PEST proteolytic Signal Containing Nuclear Protein Human Recombinant
PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.
Product # :
PRO-906Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PCNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178 a.a.) and having a molecular mass of 21.5kDa.PCNP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PCNP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
PEST proteolytic signal containing nuclear protein (PCNP) is a nuclear protein involved in cell cycle regulation and tumorigenesis. The PCNP protein is ubiquitinated post-translationally by NIRF (an ubiquitin ligase). The PCNP exists as 3 isoforms produced by alternative splicing events.
-
Synonyms
PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADGKA GDEKPEKSQR AGAAGGPEEE AEKPVKTKTV SSSNGGESSS RSAEKRSAEE EAADLPTKPT KISKFGFAIG SQTTKKASAI SIKLGSSKPK ETVPTLAPKT LSVAAAFNED EDSEPEEMPP EAKMRMKNIG RDTPTSAGPN SFNKGKHGFS DNQKLWERNI KSHLGNVHDQ DN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PECI HumanDescription:
Peroxisomal D3,D2-Enoyl-CoA Isomerase Human Recombinant
EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.
Product # :
ENZ-531Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PECI Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 42.3 kDa. The PECI is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PECI Human solution (1mg/ml) containing 20mM Tris-HCl, pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
PECI is an enzyme that localized to the peroxisomal matrix and encloses one ACB (acyl-CoA-binding) domain. PECI is expressed abundantly in liver, heart and skeletal muscle. PECI functions to catalyze the isomerization of both 3-cis and 3-trans double bonds into the 2-trans form in an array of enoyl-CoA species. PECI takes part in the beta-oxidation of unsaturated fatty acids.
-
Synonyms
EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNRTAMRASQ KDFENSMNQV KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GALM HumanDescription:
Galactose Mutarotase Human Recombinant
Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.
Product # :
ENZ-541Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GALM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-342 a.a.) and having a molecular mass of 39.9 kDa. The GALM is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GALM solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GALM is a main enzyme of carbohydrate metabolism catalysing the translation of beta-D-galactose to alpha-D-galactose. GALM is needed for normal galactose metabolism by preserveing the equilibrium of alpha and beta anomers of galactose. GALM is required for the production of complex oligosaccharides.
-
Synonyms
Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RASDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP RVLSNGVQFS RISPDGEEGY PGELKVWVTY TLDGGELIVN YRAQASQATP VNLTNHSYFN LAGQASPNIN DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LCMT1 HumanDescription:
Leucine Carboxyl Methyltransferase 1 Human Recombinant
Leucine carboxyl methyltransferase 1, LCMT1, LCMT, PPMT1, CGI-68.
Product # :
ENZ-219Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LCMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-334) and having a molecular mass of 41kDa.LCMT1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LCMT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
LCMT1 is a member of the LCMT family, methyltransferase superfamily. LCMT1 catalyzes the methylation of the carboxyl group of the C-terminal leucine residue (leu309) of the catalytic subunit of protein phosphatase-2A to form alpha-leucine ester residues.
-
Synonyms
Leucine carboxyl methyltransferase 1, LCMT1, LCMT, PPMT1, CGI-68.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMATRQR ESSITSCCST SSCDADDEGV RGTCEDASLC KRFAVSIGYW HDPYIQHFVR LSKERKAPEI NRGYFARVHG VSQLIKAFLR KTECHCQIVN LGAGMDTTFW RLKDEDLLPS KYFEVDFPMI VTRKLHSIKC KPPLSSPILE LHSEDTLQMD GHILDSKRYA VIGADLRDLS ELEEKLKKCN MNTQLPTLLI AECVLVYMTP EQSANLLKWA ANSFERAMFI NYEQVNMGDR FGQIMIENLR RRQCDLAGVE TCKSLESQKE RLLSNGWETA SAVDMMELYN RLPRAEVSRI ESLEFLDEME LLEQLMRHYC LCWATKGGNE LGLKEITY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PRMT3 HumanDescription:
Protein Arginine Methyltransferase 3 Human Recombinant
Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.
Product # :
ENZ-848Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PRMT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 554 amino acids (1-531 a.a) and having a molecular mass of 62.3kDa.PRMT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PRMT3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
PRMT3, also known as protein arginine N-methyltransferase 3, is a member of the protein arginine methyltransferase family. PRMT3 catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. PRMT3 operates on 40S ribosomal protein S2 ,rpS2, which is the major in-vivo substrate, additionally PRMT3 is also involved in the proper maturation of the 80S ribosome.
-
Synonyms
Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMCSLASG ATGGRGAVEN EEDLPELSDS GDEAAWEDED DADLPHGKQQ TPCLFCNRLF TSAEETFSHC KSEHQFNIDS MVHKHGLEFY GYIKLINFIR LKNPTVEYMN SIYNPVPWEK EEYLKPVLED DLLLQFDVED LYEPVSVPFS YPNGLSENTS VVEKLKHMEA RALSAEAALA RAREDLQKMK QFAQDFVMHT DVRTCSSSTS VIADLQEDED GVYFSSYGHY GIHEEMLKDK IRTESYRDFI YQNPHIFKDK VVLDVGCGTG ILSMFAAKAG AKKVLGVDQS EILYQAMDII RLNKLEDTIT LIKGKIEEVH LPVEKVDVII SEWMGYFLLF ESMLDSVLYA KNKYLAKGGS VYPDICTISL VAVSDVNKHA DRIAFWDDVY GFKMSCMKKA VIPEAVVEVL DPKTLISEPC GIKHIDCHTT SISDLEFSSD FTLKITRTSM CTAIAGYFDI YFEKNCHNRV VFSTGPQSTK THWKQTVFLL EKPFSVKAGE ALKGKVTVHK NKKDPRSLTV TLTLNNSTQT YGLQ
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RAC3 HumanDescription:
Ras-Related C3 Botulinum Toxin Substrate 3 Human Recombinant
Ras-related C3 substrate 3, p21-Rac3, RAC3.
Product # :
PRO-073Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RAC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 189 amino acids (1-189 a.a.) and having a total molecular mass of 21kDa.RAC3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAC3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 200mM NaCl, 0.1mM PMSF and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
RAC3 belongs to the Rac subfamily of the Rho small G proteins. RAC3 is a small (approximately 21kDa) monomeric GTP-binding protein, which is an important component of intracellular signaling pathway, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.
-
Synonyms
Ras-related C3 substrate 3, p21-Rac3, RAC3.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPHTPI LLVGTKLDLR DDKDTIERLR DKKLAPITYP QGLAMAREIG SVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKPGKKC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Description:
Hepatocyte Growth Factor Human Recombinant, HEK
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
Product # :
CYT-090Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
HGF Human Recombinant produced in HEK cells is a glycosylated disulfide-linked heterodimer, containing 697 a.a. (Gln-32 to Ser-728) having a total molecular weight of 80kDa. The HGF is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The HGF was lyophilized from a solution (1mg/ml) containing 10mM Sodium phosphate, 150mM NaCl, 0.01% Tween 80 and 100mM L-Arginine, pH 6.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.
More Info
-
Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
-
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized HGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Hepatocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728
-
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein has a total Mw of 80kDa.
What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEK.
What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728
What applications can HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.