Search results
1000 results found for “GDNF”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
VEGFR2 Fc HumanDescription:
Vascular Endothelial Growth Factor Receptor-2 Fc Chimera Human Recombinant
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Product # :
PKA-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a disulfide-linked homodimeric, glycosylated, polypeptide containing 968 amino acids and having a molecular mass of 145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.The sKDR Fc Chimera is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
KDR fusion protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH-7.2.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity of sVEGFR2/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.
More Info
-
Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. -
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized VEGFR-2 Fc/Chimera protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLK1 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 VEGFR2 in sterile water not less than 50 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ASVGLPSVSL DLPRLSIQKD ILTIKANTTL QITCRGQRDL DWLWPNNQSG SEQRVEVTEC SDGLFCKTLT IPKVIGNDTG AYKCFYRETD LASVIYVYVQ DYRSPFIASV SDQHGVVYIT ENKNKTVVIP CLGSISNLNV SLCARYPEKR FVPDGNRISW DSKKGFTIPS YMISYAGMVF CEAKINDESY QSIMYIVVVV GYRIYDVVLS PSHGIELSVG EKLVLNCTAR TELNVGIDFN WEYPSSKHQH KKLVNRDLKT QSGSEMKKFL STLTIDGVTR SDQGLYTCAA SSGLMTKKNS TFVRVHEKPF VAFGSGMESL VEATVGERVR IPAKYLGYPP PEIKWYKNGI PLESNHTIKA GHVLTIMEVS ERDTGNYTVI LTNPISKEKQ SHVVSLVVYV PPQIGEKSLI SPVDSYQYGT TQTLTCTVYA IPPPHHIHWY WQLEEECANE PSQAVSVTNP YPCEEWRSVE DFQGGNKIEV NKNQFALIEG KNKTVSTLVI QAANVSALYK CEAVNKVGRG ERVISFHVTR GPEITLQPDM QPTEQESVSL WCTADRSTFE NLTWYKLGPQ PLPIHVGELP TPVCKNLDTL WKLNATMFSN STNDILIMEL KNASLQDQGD YVCLAQDRKT KKRHCVVRQL TVLERVAPTI TGNLENQTTS IGESIEVSCT ASGNPPPQIM WFKDNETLVE DSGIVLKDGN RNLTIRRVRK EDEGLYTCQA CSVLGCAKVE AFFIIEGANA SDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSREEMT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPMLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGK.
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 :
TDP1 Human, Sf9Description:
Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant, Sf9
Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1, TDP1, FLJ11090, MGC104252.
Product # :
ENZ-1038Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 617 amino acids (1-608) and having a molecular mass of 69.5kDa. TDP1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TDP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
TDP1 belongs to the phospholipase D family and contains two PLD phosphodiesterase domains. TDP1 is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks. Mutations in the TDP1 gene are linked to the disease spinocerebellar ataxia with axonal neuropathy (SCAN1).
-
Synonyms
Tyrosyl-DNA phosphodiesterase 1, Tyr-DNA phosphodiesterase 1, TDP1, FLJ11090, MGC104252.
-
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
ADPMSQEGDY GRWTISSSDE SEEEKPKPDK PSTSSLLCAR QGAANEPRYT CSEAQKAAHK RKISPVKFSN TDSVLPPKRQ KSGSQEDLGW CLSSSDDELQ PEMPQKQAEK VVIKKEKDIS APNDGTAQRT ENHGAPACHR LKEEEDEYET SGEGQDIWDM LDKGNPFQFY LTRVSGVKPK YNSGALHIKD ILSPLFGTLV SSAQFNYCFD VDWLVKQYPP EFRKKPILLV HGDKREAKAH LHAQAKPYEN ISLCQAKLDI AFGTHHTKMM LLLYEEGLRV VIHTSNLIHA DWHQKTQGIW LSPLYPRIAD GTHKSGESPT HFKADLISYL MAYNAPSLKE WIDVIHKHDL SETNVYLIGS TPGRFQGSQK DNWGHFRLKK LLKDHASSMP NAESWPVVGQ FSSVGSLGAD ESKWLCSEFK ESMLTLGKES KTPGKSSVPL YLIYPSVENV RTSLEGYPAG GSLPYSIQTA EKQNWLHSYF HKWSAETSGR SNAMPHIKTY MRPSPDFSKI AWFLVTSANL SKAAWGALEK NGTQLMIRSY ELGVLFLPSA FGLDSFKVKQ KFFAGSQEPM ATFPVPYDLP PELYGSKDRP WIWNIPYVKA PDTHGNMWVP SHHHHHH.
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 :
CNPY4 HumanDescription:
Canopy FGF Signaling Regulator 4 Human Recombinant
PRAT4B, Protein canopy homolog 4, CNPY4.
Product # :
PRO-1976Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNPY4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (22-248 a.a) and having a molecular mass of 28.6kDa. CNPY4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques..
Source
Escherichia Coli.
Formulation
CNPY4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 5mM DTT and 2mM EDTA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Canopy FGF Signaling Regulator 4 (CNPY4) is a part of the canopy family which owns one saposin B-type domain. CNPY4 takes part in the regulation process of the cell surface expression of TLR4.
-
Synonyms
PRAT4B, Protein canopy homolog 4, CNPY4.
-
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 MGSEFGMLKE EDDDTERLPS KCEVCKLLST ELQAELSRTG RSREVLELGQ VLDTGKRKRH VPYSVSETRL EEALENLCER ILDYSVHAER KGSLRYAKGQ SQTMATLKGL VQKGVKVDLG IPLELWDEPS VEVTYLKKQC ETMLEEFEDI VGDWYFHHQE QPLQNFLCEG HVLPAAETAC LQETWTGKEI TDGEEKTEGE EEQEEEEEEE EEEGGDKMTK TGSHPKLDRE DL.
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 :
VEGF C HumanDescription:
Vascular Endothelial Growth Factor C Human Recombinant
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.
Product # :
CYT-527Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
VEGF-C Human Recombinant- contains 121 amino acids residues including 6 amino acid His-tag fused at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions.
Source
Sf9, Insect Cells.
Formulation
Each mg of VEGF-C Human contains 50mg BSA and 1xPBS as buffer.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to induce to the VEGFR-3/FLT-4 receptor phosphorylation inPAEC/VEGFR3 cells and VEGFC induced proliferation of primary HDLEC cells.
More Info
-
Introduction
VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
-
Synonyms
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized VEGF-C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-C 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 VEGF-C in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
NAA50 HumanDescription:
N Alpha-Acetyltransferase 50, NatE Catalytic Subunit Human Recombinant
N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.
Product # :
ENZ-424Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NAA50 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-169) and having a molecular mass of 21.9kDa.NAA50 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NAA50 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
N-alpha-acetyltransferase 50 (NAA50) consists of 169 amino acid cytoplasmic protein belonging to the acetyltransferase family and GNAT subfamily. NAA50 is a likely catalytic component of the ARD1A-NARG1 complex which displays alpha acetyltransferase activity. NAA50 has also been shown to interact with MAK10 and is encoded by a gene that maps to human chromosome 3q13.2.
-
Synonyms
N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.
-
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 MGSHMKGSRI ELGDVTPHNI KQLKRLNQVI FPVSYNDKFY KDVLEVGELA KLAYFNDIAV GAVCCRVDHS QNQKRLYIMT LGCLAPYRRL GIGTKMLNHV LNICEKDGTF DNIYLHVQIS NESAIDFYRK FGFEIIETKK NYYKRIEPAD AHVLQKNLKV
PSGQNADVQK TDN.
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 :
NMNAT1 HumanDescription:
Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
Product # :
ENZ-384Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NMNAT1 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT, 1mM EDTA & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.
-
Synonyms
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
-
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 KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.
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 :
SNCG HumanDescription:
Gamma-Synuclein Human Recombinant
Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.
Product # :
PRO-395Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
g-Synuclein Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 13,300 Dalton. The protein coding region of g-synuclein was amplified by RT-PCR and cloned into an E.coli expression vector. g-synuclein was overexpressed in E. coli and purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5) and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.
-
Synonyms
Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.
-
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
MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GAKTKENVVQSVTSVAEKTK EQANAVSEAV VSSVNTVATK TVEEAENIAV TSGVVRKEDL RPSAPQQEGV ASKEKEEVAE EAQSGGD.
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 :
SNUPN HumanDescription:
Snurportin 1 Human Recombinant
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
Product # :
PRO-866Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNUPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-360 a.a.) and having a molecular mass of 43.3 kDa. The SNUPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNUPN Human solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β. -
Synonyms
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
-
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 MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS
TPKLKGSSHS PDHPGCLMEN.
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 :
C12ORF5 HumanDescription:
Chromosome 12 Open Reading Frame 5 Human
Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.
Product # :
PRO-1791Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.
-
Synonyms
Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR should be stored at 4C between 2-7 days and for future use below -18C. 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 TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR
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 :
GCLM HumanDescription:
Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant
Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.
Product # :
ENZ-636Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GCLM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.
-
Synonyms
Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.
-
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 MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.
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 :
GGH HumanDescription:
Gamma-Glutamyl Hydrolase Human Recombinant
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
Product # :
ENZ-242Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GGH solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.
-
Synonyms
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
-
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 MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD
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 :
CXCL3 HumanDescription:
GRO-Gamma Human Recombinant (CXCL3)
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
Product # :
CHM-310Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GRO-Gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7902 Dalton. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
-
Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
-
Synonyms
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 CXCL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.
-
Background
What is the molecular weight/Mw of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein has a total Mw of 7.9kDa.
What is the source or expression system of CXCL3 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL3 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.
What applications can CXCL3 HUMAN Protein be used in?
CXCL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 HUMAN Protein?
The endotoxin level is minimal, CXCL3 HUMAN 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 :
CNDP2 HumanDescription:
CNDP Dipeptidase 2 Human Recombinant
Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.
Product # :
ENZ-681Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNDP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 498 amino acids (1-475) and having a molecular mass of 55.3 kDa. CNDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CNDP2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.
-
Synonyms
Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.
-
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 MGSMAALTTL FKYIDENQDR YIKKLAKWVA IQSVSAWPEK RGEIRRMMEV AAADVKQLGG SVELVDIGKQ KLPDGSEIPL PPILLGRLGS DPQKKTVCIY GHLDVQPAAL EDGWDSEPFT LVERDGKLYG RGSTDDKGPV AGWINALEAY QKTGQEIPVN VRFCLEGMEE SGSEGLDELI FARKDTFFKD VDYVCISDNY WLGKKKPCIT YGLRGICYFF IEVECSNKDL HSGVYGGSVH EAMTDLILLM GSLVDKRGNI LIPGINEAVA AVTEEEHKLY DDIDFDIEEF AKDVGAQILL HSHKKDILMH RWRYPSLSLH GIEGAFSGSG AKTVIPRKVV GKFSIRLVPN MTPEVVGEQV TSYLTKKFAE LRSPNEFKVY MGHGGKPWVS DFSHPHYLAG RRAMKTVFGV EPDLTREGGS IPVTLTFQEA TGKNVMLLPV GSADDGAHSQ NEKLNRYNYI EGTKMLAAYL YEVSQLKD.
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 :
MIF MouseDescription:
Macrophage Migration Inhibitory Factor Mouse Recombinant
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase, Glif.
Product # :
CYT-744Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa.The MIF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution containing 1mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
-
Synonyms
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase, Glif.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTNDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.
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 :
USF1 HumanDescription:
Upstream Transcription Factor 1 Human Recombinant
Upstream Transcription Factor 1, Class B Basic Helix-Loop-Helix Protein 11, Major Late Transcription Factor 1, bHLHb11, HYPLIP1, FCHL, FCHL1, MLTF, MLTFI, UEF, Upstream Stimulatory Factor 1, BHLHB11, USF, USF1.
Product # :
PRO-1783Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
USF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 333 amino acids (1-310 a.a) and having a molecular mass of 35.9kDa.USF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
USF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Upstream Transcription Factor 1 (USF1) belongs to the basic helix-loop-helix leucine zipper family, and functions as a cellular transcription factor. USF1 activates transcription via pyrimidine-rich initiator (Inr) elements and E-box motifs. The USF1 gene has been linked to familial combined hyperlipidemia (FCHL). USF1 is a transcription factor which binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') found in a various viral and cellular promoters.
-
Synonyms
Upstream Transcription Factor 1, Class B Basic Helix-Loop-Helix Protein 11, Major Late Transcription Factor 1, bHLHb11, HYPLIP1, FCHL, FCHL1, MLTF, MLTFI, UEF, Upstream Stimulatory Factor 1, BHLHB11, USF, USF1.
-
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 MGSMKGQQKT AETEEGTVQI QEGAVATGED PTSVAIASIQ SAATFPDPNV KYVFRTENGG QVMYRVIQVS EGQLDGQTEG TGAISGYPAT QSMTQAVIQG AFTSDDAVDT EGTAAETHYT YFPSTAVGDG AGGTTSGSTA AVVTTQGSEA LLGQATPPGT GQFFVMMSPQ EVLQGGSQRS IAPRTHPYSP KSEAPRTTRD EKRRAQHNEV ERRRRDKINN WIVQLSKIIP DCSMESTKSG QSKGGILSKA CDYIQELRQS NHRLSEELQG LDQLQLDNDV LRQQVEDLKN KNLLLRAQLR HHGLEVVIKN DSN.
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 :
GH Antagonist RatDescription:
Growth Hormone Anatagonist Rat Recombinant
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-1250Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Rat Growth Hormone Anatagonist produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. GH Antagonist Rat is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045M NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by Gel Filtration.
(c) Analysis by SDS-PAGE.
Biological Activity
Plays a role as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain and binds to this ECD with affinity similar the the wild type rGH.
More Info
-
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GH Antagonist Rat although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 GH Antagonist Rat in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Phe-Pro-Ala-Met.
-
Background
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with 4 other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which was evolved by a series of gene duplications. The 5 genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the 5 growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other 4 genes in the growth hormone locus.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman analysis program of protein sequences.
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 :
AGA Human, sf9Description:
Aspartylglucosaminidase Human Recombinant, sf9
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
Product # :
ENZ-990Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
-
Synonyms
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
-
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
ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH HH.
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 :
NAGA HumanDescription:
N-Acetylgalactosaminidase Alpha Human Recombinant
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
Product # :
ENZ-963Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NAGA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 400 amino acids (18-411) and having a molecular mass of 45.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NAGA is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NAGA protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
N-Acetylgalactosaminidase Alpha (NAGA) is a lysosomal exoglycosidase which removes terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. NAGA is necessary for the breakdown of glycolipids.
-
Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
-
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
LDNGLLQTPP MGWLAWERFR CNINCDEDPK NCISEQLFME MADRMAQDGW RDMGYTYLNI DDCWIGGRDA SGRLMPDPKR FPHGIPFLAD YVHSLGLKLG IYADMGNFTC MGYPGTTLDK VVQDAQTFAE WKVDMLKLDG CFSTPEERAQ GYPKMAAALN ATGRPIAFSC SWPAYEGGLP PRVNYSLLAD ICNLWRNYDD IQDSWWSVLS ILNWFVEHQD ILQPVAGPGH WNDPDMLLIG NFGLSLEQSR AQMALWTVLA APLLMSTDLR TISAQNMDIL QNPLMIKINQ DPLGIQGRRI HKEKSLIEVY MRPLSNKASA LVFFSCRTDM PYRYHSSLGQ LNFTGSVIYE AQDVYSGDII SGLRDETNFT VIINPSGVVM WYLYPIKNLE MSQQHHHHHH.
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 :
GOT2 Mouse, ActiveDescription:
Glutamic-Oxaloacetic Transaminase 2, Active Mouse Recombinant
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV, Kynurenine Aminotransferase 4.
Product # :
ENZ-1111Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GOT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (30-430 aa) and having a molecular mass of 46.8kDa.GOT2 is fused to a 21 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH7.4)
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 20 units/mg. Measured by the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C˚.
More Info
-
Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 participates in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.
-
Synonyms
Transaminase A, KAT4, KATIV, KAT-4, KAT-IV, Kynurenine Aminotransferase 4.
-
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 MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR
DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT
VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG
FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG
FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL
KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS
HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV TK
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 :
GPT2 Mouse, ActiveDescription:
Glutamic-Pyruvate Transaminase 2, Active Mouse Recombinant
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
Product # :
ENZ-1110Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GPT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 542 amino acids (1-522 aa) and having a molecular mass of 60.1kDa.GPT2 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPT2 solution (1 mg/ml) contains 2mM DTT, 20% Glycerol and 20mM Tris-HCl (pH7.5).
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 50 units/mg. Measured by the amount of enzyme that cleaves 1umole of L-Alanineto L-Glutamate per minute at pH7.5 at 37C˚.
More Info
-
Introduction
Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.
-
Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE
RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA
MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR
EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA
VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC
IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK
GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ
FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA
PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ YS
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 :
GPX2 HumanDescription:
Glutathione Peroxidase 2 Human Recombinant
Glutathione peroxidase 2, GPx-2, GSHPx-2, Gastrointestinal glutathione peroxidase, Glutathione peroxidase-gastrointestinal, GPx-GI, GSHPx-GI, Glutathione peroxidase-related protein 2, GPRP-2, GPX2, GPRP, GI-GPx.
Product # :
ENZ-206Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GPX2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190) and having a molecular mass of 24.1kDa.GPX2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPX2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Glutathione peroxidase 2 (GPX2) is a member of the glutathione peroxidase family, consisting of 8 known glutathione peroxidases (Gpx1-8) in humans. Glutathione peroxidase functions in the detoxification of hydrogen peroxide, and is one of the most important antioxidant enzymes in humans. GPX2 may have a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. GPX2 is one of only a few proteins known in higher vertebrates to contain selenocysteine, which appears at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA.
-
Synonyms
Glutathione peroxidase 2, GPx-2, GSHPx-2, Gastrointestinal glutathione peroxidase, Glutathione peroxidase-gastrointestinal, GPx-GI, GSHPx-GI, Glutathione peroxidase-related protein 2, GPRP-2, GPX2, GPRP, GI-GPx.
-
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 MAFIAKSFYD LSAISLDGEK VDFNTFRGRA VLIENVASLC GTTTRDFTQL NELQCRFPRR LVVLGFPCNQ FGHQENCQNE EILNSLKYVR PGGGYQPTFT LVQKCEVNGQ NEHPVFAYLK DKLPYPYDDP FSLMTDPKLI IWSPVRRSDV AWNFEKFLIG PEGEPFRRYS RTFPTINIEP DIKRLLKVAI.
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 :
EIF1AX HumanDescription:
Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
Product # :
PRO-253Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.
-
Synonyms
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
-
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 MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI
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 :
Epigen HumanDescription:
Epigen Human Recombinant
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Product # :
CYT-601Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epigen Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa. Epigen is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EPGN was lyophilized from 20mM PBS buffer pH-7.4 .
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.
More Info
-
Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
-
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epigen although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPGN 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 Epigen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
-
Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 7.9kDa.
What is the source or expression system of EPIGEN Protein?
Escherichia Coli.
What is the Purity of EPIGEN Protein?
EPIGEN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPIGEN Protein?
Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.
What is the amino acid sequence of EPIGEN Protein?
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN 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 :
C1QTNF7 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 7 Human Recombinant
CTRP7, C1QTNF7, ZACRP7, Complement C1q tumor necrosis factor-related protein 7.
Product # :
PRO-514Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
C1QTNF7 Human Recombinant produced in E.Coli is a signle, non-glycosylated, Polypeptide chain containing 283 amino acids and having a molecular mass of 30.22 kDa. The protein contains an extra 10 amino acid His tag at N-terminus. The C1QTNF7 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ2 amino acids 17–289.The C1QTNF7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human C1QTNF7 was filtered (0.4µm) and lyophilized from a 0.5mg/ml solution containing 30mM Acetate Buffer, pH-4 and 5% (w/v) trehalose.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
-
Introduction
C1QTNF7 is a collagen type-IV specific for basement membranes.
-
Synonyms
CTRP7, C1QTNF7, ZACRP7, Complement C1q tumor necrosis factor-related protein 7.
-
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
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHAS QPRGNQLKGE NYSPRYICSI PGLPGPPGPP GANGSPGPHG RIGLPGRDGR DGRKGEKGEK GTAGLRGKTG PLGLAGEKGD QGETGKKGPI GPEGEKGEVG PIGPPGPKGD RGEQGDPGLP GVCRCGSIVL KSAFSVGITT SYPEERLPII FNKVLFNEGE HYNPATGKFI CAFPGIYYFS YDITLANKHL AIGLVHNGQY RIKTFDANTG NHDVASGSTV IYLQPEDEVW LEIFFTDQNG LFSDPGWADS LFSGFLLYVD TDYLDSISEDDEL.
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.