Search results
1000 results found for “visfatin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
ANXA10 HumanDescription:
Annexin A10 Human Recombinant
Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.
Product # :
PRO-1045Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ANXA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-324 a.a.) and having a molecular mass of 39.8kDa.ANXA10 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANXA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Annexin A10 (ANXA10) is a member of the annexin family of calcium-binding proteins that contains a few members which are described by a conserved core domain that binds phospholipids in a Ca2+-dependent manner, and a unique amino-terminal region, which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and might be required in the regulation of cellular growth and signal transduction pathways throughout the cell.
-
Synonyms
Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.
-
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 MGSHMFCGDY VQGTIFPAPN FNPIMDAQML GGALQGFDCD KDMLINILTQ RCNAQRMMIA EAYQSMYGRD LIGDMREQLS DHFKDVMAGL MYPPPLYDAH ELWHAMKGVG TDENCLIEIL ASRTNGEIFQ MREAYCLQYS NNLQEDIYSE TSGHFRDTLM
NLVQGTREEG YTDPAMAAQD AMVLWEACQQ KTGEHKTMLQ MILCNKSYQQ LRLVFQEFQN ISGQDMVDAI NECYDGYFQE LLVAIVLCVR DKPAYFAYRL YSAIHDFGFH NKTVIRILIA RSEIDLLTIR KRYKERYGKS LFHDIRNFAS GHYKKALLAI CAGDAEDY.
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 :
NDUFA4 HumanDescription:
NADH Dehydrogenase1 Alpha Subcomplex 4 Human Recombinant
NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.
Product # :
ENZ-803Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
NDUFA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids (1-81 a.a) and having a molecular mass of 11.8kDa. NDUFA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NDUFA4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NADH Dehydrogenase1 Alpha Subcomplex 4 (NDUFA4) is a member of the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is comprised of 45 different subunits. NDUFA4 protein has NADH dehydrogenase activity and oxidoreductase activity. NDUFA4 transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the NDUFA4 enzyme is assumed to be ubiquinone.
-
Synonyms
NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.
-
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 MGSMLRQIIG QAKKHPSLIP LFVFIGTGAT GATLYLLRLA LFNPDVCWDR NNPEPWNKLG PNDQYKFYSV NVDYSKLKKE RPDF.
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 :
NFNB E.ColiDescription:
Dihydropteridine Reductase E.Coli Recombinant
DPRA, NFSB, NFSI, NTR.
Product # :
ENZ-423Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
NFNB Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 26 kDa. The NFNB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.
-
Synonyms
DPRA, NFSB, NFSI, NTR.
-
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 MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV.
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 :
EFNB3 HumanDescription:
Ephrin- B3 Human Recombinant
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
Product # :
PRO-1169Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.
-
Synonyms
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
-
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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.
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 :
NTS HumanDescription:
Neurotensin Human Recombinant
NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.
Product # :
PRO-1311Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
NTS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (24-170 a.a.) and having a molecular mass of 19.9kDa.NTS is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
-
Synonyms
NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.
-
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 MGSHMSDSEE EMKALEADFL TNMHTSKISK AHVPSWKMTL LNVCSLVNNL NSPAEETGEV HEEELVARRK LPTALDGFSL EAMLTIYQLH KICHSRAFQH WELIQEDILD TGNDKNGKEE VIKRKIPYIL KRQLYENKPR RPYILKRDSY YY.
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 :
Eotaxin Human, HisDescription:
Eotaxin Human Recombinant (CCL11), His Tag
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-344Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Eotaxin His Tag Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids fragment (24-87) corresponding to the mature Eotaxin protein and having a molecular mass of 8345.9 Dalton with an amino-terminal hexahistidine tag.The Eotaxin-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Eotaxin-His is supplied liquid In Phosphate Buffered Saline pH7.4 containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE
Citations
More Info
-
Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
-
Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
-
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. Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
-
Background
What is the molecular weight/Mw of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein has a total Mw of 8.34kDa.
What is the source or expression system of EOTAXIN HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN, HIS Protein?
The biological functionality of EOTAXIN HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of EOTAXIN HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
What applications can EOTAXIN HUMAN, HIS Protein be used in?
EOTAXIN HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN, HIS Protein?
The endotoxin level is minimal, EOTAXIN HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant EOTAXIN HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of EOTAXIN HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
OPTC HumanDescription:
Opticin Human Recombinant
Opticin, Oculoglycan, OPT.
Product # :
PRO-2151Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
OPTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (20-332 a.a) and having a molecular mass of 37.6kDa. OPTC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OPTC protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Opticin also known as OPTC is a member of the class III of the small leucine-rich repeat protein (SLRP) family. Members of this family are usually linked with the extracellular matrix. OPTC is attended in significant quantities in the vitreous of the eye and also localizes to the cornea, iris, ciliary body, optic nerve, choroid, retina, and fetal liver. OPTC might noncovalently bind collagen fibrils and regulate fibril morphology, spacing and organization. OPTC is mapped to a an area of chromosome 1 which is linked with the inherited eye diseases age-related macular degeneration (AMD) and posterior column ataxia with retinosa pigmentosa (AXPC1).
-
Synonyms
Opticin, Oculoglycan, OPT.
-
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 MGSASLPRKE RKRREEQMPR EGDSFEVLPL RNDVLNPDNY GEVIDLSNYE ELTDYGDQLP EVKVTSLAPA TSISPAKSTT APGTPSSNPT MTRPTTAGLL LSSQPNHGLP TCLVCVCLGS SVYCDDIDLE DIPPLPRRTA YLYARFNRIS RIRAEDFKGL TKLKRIDLSN NLISSIDNDA FRLLHALQDL ILPENQLEAL PVLPSGIEFL DVRLNRLQSS GIQPAAFRAM EKLQFLYLSD NLLDSIPGPL PLSLRSVHLQ NNLIETMQRD VFCDPEEHKH TRRQLEDIRL DGNPINLSLF PSAYFCLPRL PIGRFT.
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 :
STMN1 HumanDescription:
Stathmin-1 Human Recombinant
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
Product # :
PRO-676Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Human Stathmin-1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149 a.a) and having a molecular mass of 19.4 kDa. STMN1 is fused to 20 amino acid His Tga at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN1 protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
STMN1 takes part in the regulation of the microtubule filament structure by destabilizing microtubules. STMN1 promotes the disassembly of microtubules and prevents assembly. STMN1 is a ubiquitous cytosolic phosphoprotein which functions as an intracellular relay integrating regulatory signals of the cellular environment. Stathmin functions as an Oncoprotein in regulation of the cell cycle. Stathmin mutation results in uncontrolled cell proliferation. Stathmin expression associates with cervical carcinogenesis and tumor progression, thus Stathmin is an important prognostic marker in cervical carcinoma. STMN1, takes part in the prevenative progression of ER-positive primary in breast cancer. Somatic mutation in STMN1 effects cell homeostasis that leads to tumorigenicity.
-
Synonyms
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
-
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 MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL ERLREKDKHI EEVRKNKESK DPADETEAD.
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 :
OTOR HumanDescription:
Otoraplin Human Recombinant
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
Product # :
CYT-582Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR 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 Otoraplin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
DIDFFCE.
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 :
bNGF Human, CHODescription:
Beta-Nerve Growth Factor Human Recombinant, CHO
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Product # :
CYT-246Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Nerve Growth Factor-beta Human Recombinant produced in CHO is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.The NGF-b is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells.
Formulation
The protein was lyophilized from a 0.2µm filtered solution in 20mM PB and 250mM NaCl, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.Citations
More Info
-
Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
-
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Nerve Growth Factor b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Nerve Growth Factor-beta 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 NGF-b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Was analyzed by Mass spectrometry.
-
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.
What is the source or expression system of B NGF Protein?
Chinese Hamster Ovary Cells.
What is the Purity of B NGF Protein?
B NGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of B NGF Protein?
The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.
What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.
What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF 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 :
BPIFA1 HumanDescription:
BPI fold containing family A Member 1 Human Recombinant
BPI fold-containing family A member 1, Lung-specific protein X, Nasopharyngeal carcinoma-related protein, Palate lung and nasal epithelium clone protein, Secretory protein in upper respiratory tracts, Tracheal epithelium-enriched protein, Von Ebner protein Hl, BPIFA1, LUNX, NASG, PLUNC, SPURT, SPLUNC1, bA49G10.5.
Product # :
PRO-404Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
BPIFA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (20-256 a.a) and having a molecular mass of 27.1kDa.BPIFA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BPIFA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BPI fold containing family A Member 1 (BPIFA1) belongs to the short subfamily of PLUNC family proteins and have homology only to the Nterminal domains of BPI. BPIFA1 is a secreted protein which is expressed in the secretory ducts and submucosal glands of tracheobronchial tissues. BPIFA1 binds to LPS (lipopolysaccharide) in nasal lavage fluid (NLF) which alludes to its role in the inflammatory response of the upper airways after exposure to irritants. BPIFA1 may also serve as a potential molecular marker for detection of micrometastasis in non-small-cell lung cancer. Decreased levels of BPIFA1 are observed in the NLF of smokers and people who have been exposed to reactive epoxy chemicals, which indicats that long-term exposure to airway irritants damages the production of BPIFA1 in the upper respiratory tract.
-
Synonyms
BPI fold-containing family A member 1, Lung-specific protein X, Nasopharyngeal carcinoma-related protein, Palate lung and nasal epithelium clone protein, Secretory protein in upper respiratory tracts, Tracheal epithelium-enriched protein, Von Ebner protein Hl, BPIFA1, LUNX, NASG, PLUNC, SPURT, SPLUNC1, bA49G10.5.
-
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 MGSQFGGLPV PLDQTLPLNV NPALPLSPTG LAGSLTNALS NGLLSGGLLG ILENLPLLDI LKPGGGTSGG LLGGLLGKVT SVIPGLNNII DIKVTDPQLL ELGLVQSPDG HRLYVTIPLG IKLQVNTPLV GASLLRLAVK LDITAEILAV RDKQERIHLV LGDCTHSPGS LQISLLDGLG PLPIQGLLDS LTGILNKVLP ELVQGNVCPL VNEVLRGLDI TLVHDIVNML IHGLQFVIKV.
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 :
FAM84B HumanDescription:
Family with Sequence Similarity 84, Member B Human Recombinant
FAM84B, Family with Sequence Similarity 84 Member B, BCMP101, Breast Cancer Membrane-Associated Protein 101, Neurological/Sensory 2, Breast Cancer Membrane Protein 101, NSE2, Protein FAM84B, Protein NSE2.
Product # :
PRO-1779Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
FAM84B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 333 amino acids (1-310) and having a molecular mass of 36.9kDa.FAM84B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FAM84B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Family with Sequence Similarity 84, Member B (FAM84B) coprecipitated with a downstream effector of RAS, CRAF. Binding of FAM83B with CRAF interrupted CRAF/14-3-3 interactions and increased CRAF membrane localization, causing elevated MAPK and mammalian target of rapamycin (mTOR) signaling. FAM84B is an oncogene and possibly represents a new target for therapeutic intervention.
-
Synonyms
FAM84B, Family with Sequence Similarity 84 Member B, BCMP101, Breast Cancer Membrane-Associated Protein 101, Neurological/Sensory 2, Breast Cancer Membrane Protein 101, NSE2, Protein FAM84B, Protein NSE2.
-
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 MGSMGNQVEK LTHLSYKEVP TADPTGVDRD DGPRIGVSYI FSNDDEDVEP QPPPQGPDGG GLPDGGDGPP PPQPQPYDPR LHEVECSVFY RDECIYQKSF APGSAALSTY TPENLLNKCK PGDLVEFVSQ AQYPHWAVYV GNFQVVHLHR LEVINSFLTD ASQGRRGRVV NDLYRYKPLS SSAVVRNALA HVGAKERELS WRNSESFAAW CRYGKREFKI GGELRIGKQP YRLQIQLSAQ RSHTLEFQSL EDLIMEKRRN DQIGRAAVLQ ELATHLHPAE PEEGDSNVAR TTPPPGRPPA PSSEEEDGEA VAH.
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 :
FGF 8 MouseDescription:
Fibroblast Growth Factor-8 Mouse Recombinant
Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.
Product # :
CYT-070Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.The FGF-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGF-8 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.Citations
More Info
-
Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
-
Synonyms
Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 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 FGF-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.
-
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 28.1kDa.
What is the source or expression system of FGF8 Protein?
Escherichia Coli.
What is the Purity of FGF8 Protein?
FGF8 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF8 Protein?
The ED50, as determined by the dose-dependent a cell proliferation assay using NR6R-3T3 mouse fibroblast cells is <25 ng/ml in the presence of 0.1 ug/ml heprin, corresponding to a specific activity of > 4.0×104 units/mg.
What is the amino acid sequence of FGF8 Protein?
QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.
What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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 :
CALB2 HumanDescription:
Calbindin-2 Human Recombinant
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
Product # :
PRO-401Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.
-
Synonyms
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
-
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 MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.
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 :
KRT19 Human, HisDescription:
Cytokeratin 19 Human Recombinant , His Tag
Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.
Product # :
PRO-1347Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
KRT19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 46.5kDa.KRT19 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KRT19 solution (0.5mg/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.
Citations
More Info
-
Introduction
CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.
-
Synonyms
Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.
-
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 avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSYSYR QSSATSSFGG LGGGSVRFGP GVAFRAPSIH GGSGGRGVSV SSARFVSSSS SGAYGGGYGG VLTASDGLLA GNEKLTMQNL NDRLASYLDK VRALEAANGE LEVKIRDWYQ KQGPGPSRDY SHYYTTIQDL RDKILGATIE NSRIVLQIDN ARLAADDFRT KFETEQALRM SVEADINGLR RVLDELTLAR TDLEMQIEGL KEELAYLKKN HEEEISTLRG QVGGQVSVEV DSAPGTDLAK ILSDMRSQYE VMAEQNRKDA EAWFTSRTEE LNREVAGHTE QLQMSRSEVT DLRRTLQGLE IELQSQLSMK AALEDTLAET EARFGAQLAH IQALISGIEA QLGDVRADSE RQNQEYQRLM DIKSRLEQEI ATYRSLLEGQ EDHYNNLSAS KVL.
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 :
LECT1 HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1846Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
-
Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
-
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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.
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 :
PSMD11 HumanDescription:
Proteasome 26S Subunit, Non-ATPase 11 Human Recombinant
S9, Rpn6, p44.5, MGC26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit p44.5, PSMD11.3844, 26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit RPN6.
Product # :
ENZ-760Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
PSMD11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 442 amino acids (1-422a.a) and having a molecular mass of 49.6kDa. PSMD11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PSMD11 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
The 26S proteasome is a multicatalytic proteinase complex with a well ordered structure composed of two complexes- a 20S core and a 19S regulator. PSMD11 is a non-ATPase subunit of the 19S regulator. The 20S core is composed of four rings of 28 non-identical subunits; two rings are composed of 7 alpha subunits and two rings are composed of 7 beta subunits. The 19S regulator is composed of a base that contains six ATPase subunits and two non-ATPase subunits, and a lid that contains up to ten non-ATPase subunits. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An indispensable function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.
-
Synonyms
S9, Rpn6, p44.5, MGC26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit p44.5, PSMD11.3844, 26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit RPN6.
-
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 MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK LT.
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 :
FGF 2 Human, sf9Description:
Fibroblast Growth Factor-Basic Human Recombinant, Sf9
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-365Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.
Source
Baculovirus.
Formulation
The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.Citations
More Info
-
Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
-
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
-
Physical Appearance
Sterile Filtered liquid formulation.
-
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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
-
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.
What is the source or expression system of FGF 2 Protein?
Baculovirus.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.
What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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 :
SUMF1 HumanDescription:
Sulfatase Modifying Factor 1 Human Recombinant
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
Product # :
PRO-986Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
SUMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (91-374 a.a.) and having a molecular mass of 34.1kDa.SUMF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SUMF1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2M UREA, 2mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
SUMF1 is a member of the SUMF family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Alterations in this gene result in multiple sulfatase deficiency which is a lysosomal storage disorder.
-
Synonyms
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
-
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 MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE TSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD
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 :
BST1 HumanDescription:
Bone Marrow Stromal Cell Antigen 1 Human Recombinant
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.
Product # :
CYT-1071Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.
-
Synonyms
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 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
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
-
Background
The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine
Introduction
In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.
BST-1: A Versatile Player
BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.
Engineering a Cellular Conductor
With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.
Entering the Biological Stage
Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.
An Enthusiastic Applause for Results
Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.
Conclusion
The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST1 Protein?
BST1 Protein has a total Mw of 30.5kDa.
What is the source or expression system of BST1 Protein?
Sf9, Baculovirus cells.
What is the Purity of BST1 Protein?
BST1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BST1 Protein?
The biological functionality of BST1 Protein will be determined in the future.
What is the amino acid sequence of BST1 Protein?
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
What applications can BST1 Protein be used in?
BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BST1 Protein?
The endotoxin level is minimal, BST1 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 :
PFDN2 HumanDescription:
Prefoldin Subunit 2 Human Recombinant
Prefoldin subunit 2, PFDN2, PFD2.
Product # :
PRO-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
PFDN2 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 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Prefoldin subunit 2 (PFDN2) belongs to the prefoldin beta subunit family. The PFDN2 protein is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold correctly. PFDN2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.
-
Synonyms
Prefoldin subunit 2, PFDN2, PFD2.
-
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 MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.
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 :
CX3CL1 Human, HisDescription:
Fractalkine Human Recombinant (CX3CL1), His Tag
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-360Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
- Citations
Description
Fractalkine 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 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
-
Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
-
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
-
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 MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
-
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.
What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
What applications can CX3CL1 HUMAN, HIS Protein be used in?
CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CX3CL1 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CX3CL1 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
TNFRSF4 HumanDescription:
TNF Receptor Superfamily Member 4 Human Recombinant
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
Product # :
CYT-1039Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
TNFRSF4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 425 amino acids (29-214a.a.) and having a molecular mass of 46.9Da. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF4 is expressed with a 239 amino acid higG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with mouse OX40 Ligand/TNFSF4 The ED50 range ≤ 0.15 ug/ml.
Citations
More Info
-
Introduction
TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.
-
Synonyms
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
-
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
LHCVGDTYPS NDRCCHECRP GNGMVSRCSR SQNTVCRPCG PGFYNDVVSS KPCKPCTWCN LRSGSERKQL CTATQDTVCR CRAGTQPLDS YKPGVDCAPC PPGHFSPGDN QACKPWTNCT LAGKHTLQPA SNSSDAICED RDPPATQPQE TQGPPARPIT VQPTEAWPRT SQGPSTRPVE VPGGRALEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH
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 :
GFRA1 HumanDescription:
GDNF Family Receptor Alpha 1 Human Recombinant
GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.
Product # :
CYT-1026Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).
Source
HEK293 cells.
Formulation
GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
-
Synonyms
GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.
-
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 two weeks 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. GFRA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.
-
Background
What is the molecular weight/Mw of GFRA1 Protein?
GFRA1 Protein has a total Mw of 46kDa.
What is the source or expression system of GFRA1 Protein?
HEK293 cells.
What is the Purity of GFRA1 Protein?
GFRA1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GFRA1 Protein?
The biological functionality of GFRA1 Protein will be determined in the future.
What is the amino acid sequence of GFRA1 Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.
What applications can GFRA1 Protein be used in?
GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GFRA1 Protein?
The endotoxin level is minimal, GFRA1 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.