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1000 results found for “vegf protein”
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Name :
Noggin Human, Sf9Description:
Noggin Human Recombinant, Sf9
SYM1, SYNS1, NOG.
Product # :
CYT-1119Price :
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Shipped at Room temp
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Description
Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.
More Info
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Introduction
Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Noggin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.
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.
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Name :
FAM3D HumanDescription:
Family with Sequence Similarity 3, Member D Human Recombinant
Protein FAM3D, FAM3D, EF7, OIT1.
Product # :
PRO-1585Price :
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Shipped at Room temp
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Description
FAM3D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-224) containing 209 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 23.3kDa (calculated).
Source
Escherichia Coli.
Formulation
FAM3D filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Family with Sequence Similarity 3, Member D (FAM3D) is a member of the FAM3 family. The FAM3D gene is linked to narcolepsy and diabetes mellitus in pancreatic adenocarcinoma, however FAM3D function of remains vague. FAM3D is amply expressed in the placenta and weakly expressed in the small intestine.
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Synonyms
Protein FAM3D, FAM3D, EF7, OIT1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. 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. FAM3D is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASYMSFSMKTIR LPRWLAASPT KEIQVKKYKC GLIKPCPANY FAFKICSGAA NVVGPTMCFE DRMIMSPVKN NVGRGLNIAL VNGTTGAVLG QKAFDMYSGD VMHLVKFLKE IPGGALVLVA SYDDPGTKMN DESRKLFSDL GSSYAKQLGF RDSWVFIGAK DLRGKSPFEQ FLKNSPDTNK YEGWPELLEM EGCMPPKPF.
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.
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Name :
RNF4 HumanDescription:
Ring Finger Protein 4 Human Recombinant
E3 ubiquitin-protein ligase RNF4, RING finger protein 4, Small nuclear ring finger protein, Protein SNURF, RNF4, SNURF, RES4-26, SLX5.
Product # :
PRO-1255Price :
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Description
RNF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 23.7kDa.RNF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNF4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
E3 ubiquitin ligase RNF4 (RNF4) contains a RING finger motif and functions as a transcription regulator. RNF4 interacts with, and inhibits the activity of, TRPS1, a transcription suppressor of GATA-mediated transcription. Transcription repressor ZNF278/PATZ also interacts with the RNF4 protein thus reducing the enhancement of androgen receptor-dependent transcription mediated by RNF4. RNF4 is broadly expressed at low levels in many tissues and highly expressed in the testis.
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Synonyms
E3 ubiquitin-protein ligase RNF4, RING finger protein 4, Small nuclear ring finger protein, Protein SNURF, RNF4, SNURF, RES4-26, SLX5.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSTRKRR GGAINSRQAQ KRTREATSTP EISLEAEPIE LVETAGDEIV DLTCESLEPV VVDLTHNDSV VIVDERRRPR RNARRLPQDH ADSCVVSSDD EELSRDRDVY VTTHTPRNAR DEGATGLRPS GTVSCPICMD GYSEIVQNGR LIVSTECGHV FCSQCLRDSL KNANTCPTCR KKINHKRYHP IYI.
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.
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Name :
GFRA3 HumanDescription:
GDNF Family Receptor Alpha 3 Human Recombinant
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.
Product # :
CYT-399Price :
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Shipped with Ice Packs
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Description
GFRA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (32-374a.a) and having a molecular mass of 40.7kDa.GFRA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GFRA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
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Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN
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Background
What is the molecular weight/Mw of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein has a total Mw of 40.7kDa.
What is the source or expression system of GFRA3 HUMAN Protein?
Escherichia Coli.
What is the Purity of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GFRA3 HUMAN Protein?
The biological functionality of GFRA3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GFRA3 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN
What applications can GFRA3 HUMAN Protein be used in?
GFRA3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GFRA3 HUMAN Protein?
The endotoxin level is minimal, GFRA3 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.
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Name :
CBFB HUmanDescription:
Core Binding Factor Beta Human Recombinant
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
Product # :
PRO-534Price :
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Shipped with Ice Packs
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Description
CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.
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Synonyms
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
REEMEVRVSQ LLAVTGKKTT RP.
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.
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Name :
Ebola Zaire ProteinDescription:
Ebola Zaire Recombinant Protein
Product # :
EVD-078Price :
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Shipped with Ice Packs
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Description
Nucleoprotein (NP) of Ebola virus has strong antigenicity in immune reactions. C-terminal of EBO-Z nucleoprotein was expressed and purified from E. coli, it migrated at 15kDa on SDS-PAGE and pI is 4.87. Ebola Zaire is fused to a c-terminal his tag and purified by a proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Ebola Zaire protein solution is supplied in Phosphate buffer and 0.02% sodium azide.
Purity
>95% pure as determined by 12% SDS-PAGE (Coomassie blue stain).
More Info
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Introduction
Ebolavirus (EVD) belongs to the Filoviridae family of proteins which is comprised of a single-strand, non-infectious RNA genome. EVD genome is about 19,000 base pairs long and covers 7 genes in the order 3'-UTR-NP-VP35-VP40-GP-VP30-VP24-L-5'-UTR. There are 4 different ebolaviruses such as: Zaire (EBO-Z), Sudan (EBO-S), Cote d’Ivoire (EBO-CI) and Reston (EBO-R) that differ in amino acid sequence and location of where the gene overlaps. Similar to filoviruses and ebolavirions, EVD is a filamentous element that could appear in 3 forms: shepherd's crook, U shape or a 6 shape. Ebolaviruses may be coiled, toroid, or branched. Most ebolavirions are 80nm wideand 14,000nm long.
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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.
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Applications
Immunoassay.
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.
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Name :
GHRL ProteinDescription:
Ghrelin Human
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-297Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ghrelin Human contains 28 amino acids and a total molecular mass of 3370.9 Dalton and a molecular formula of C149H249N47O42.The GHRL is purified by proprietary chromatographic techniques.
Formulation
GHRL was lyophilized without additives.
Purity
Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
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Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
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Physical Appearance
Sterile Filtered Yellowish lyophilized (freeze-dried) powder that may appear as a gel form.
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Stability
Store the lyophilized Ghrelin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GHRL can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to a working concentration approximately 0.5mg/1ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.
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.
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Name :
Visfatin Human, HisDescription:
Visfatin Recombinant Human, His Tag
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
CYT-563Price :
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Shipped with Ice Packs
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Description
Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids and having a molecular mass of 57 kDa. The recombinant human Visfatin is fused to His tag at N-Terminus.
Source
Escherichia Coli.
Formulation
Visfatin His tag protein contains 20mM Tris pH-8, 0.1mM DTT & 10% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-?, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established.
Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes. -
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Physical Appearance
Sterile Filtered solution at a concentration of 1mg/ml.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG WNYILEKYDG HLPIEIKAVP EGFVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA QLNIELEAAH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OPG Fc HumanDescription:
Osteoprotegerin Human Recombinant /Fc Chimera
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
Product # :
CYT-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant OPG produced in yeast contains 2x412 amino acid residues, including 180 residues from mature OPG (a.a 22-201) and 232 residues from the Fc protein of human IgG1, and has a calculated molecular mass of 109.6kDa.
Source
Pichia Pastoris.
Formulation
OPG was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 6.0, 150mM NaCl and 0.02 % Tween-80.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by neutralizing the stimulation of U937 cells is less tha10ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10ng/ml soluble Human RANKL (sRANKL).
More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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.
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Solubility
It is recommended to reconstitute the lyophilized Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
OPG 22-201 ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL
Fc232EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKTISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK
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.
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Name :
GMFB RatDescription:
Glia Maturation Factor Beta Rat Recombinant
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
Product # :
CYT-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glia Maturation Factor-Beta (GMF-Beta) Rat Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
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Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GMFB although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution GMFB 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 GMFB in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDKR LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPLGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
-
Background
What is the molecular weight/Mw of GMFB RAT Protein?
GMFB RAT Protein has a total Mw of 16.6kDa.
What is the source or expression system of GMFB RAT Protein?
Escherichia Coli.
What is the Purity of GMFB RAT Protein?
GMFB RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GMFB RAT Protein?
The biological functionality of GMFB RAT Protein will be determined in the future.
What is the amino acid sequence of GMFB RAT Protein?
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDKR LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPLGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
What applications can GMFB RAT Protein be used in?
GMFB RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GMFB RAT Protein?
The endotoxin level is minimal, GMFB RAT 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 :
CST3 Protein, HisDescription:
Cystatin-C Human Recombinant, His Tag
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-656Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
-
Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
-
Synonyms
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- More Info
Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
More Info
-
Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
-
Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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 Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.
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 :
StreptavidinDescription:
Streptavidin Recombinant
Product # :
PRO-791Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.
Source
Escherichia Coli.
Formulation
Lyophilized in 10mM potassium phosphate buffer pH 6.5.
Purity
Greater than 98.0% as determined by SDS-PAGE and HPLC.
More Info
-
Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.
-
Solubility
It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS. -
Proteolytic Activity
< 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).
-
Specific Activity
> 17U/mg (one unit binds 1 μg D-biotin).
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 :
MANF Human, HisDescription:
Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag
Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.
Product # :
CYT-133Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.
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Synonyms
Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL
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 :
hCG ProteinDescription:
Chorionic Gonadotropin Human
Chorionic gonadotropin, hCG, CG.
Product # :
HOR-250Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- biological activity
- More Info
- Activity Assay
Description
Human Chorionic Gonadotropin is produced from a sterile preparation of placental glucoprotein urine of pregnant women having a total molecular mass of 36,700 Dalton. The hCG consists of 237 amino acids, a chain-92 amino acids and b chain-145 amino acids. The hCG is purified by proprietary chromatographic techniques.
Source
Urine of pregnant women.
Formulation
The hCG was lyophilized with no additives.
Biological Activity
The activity was found to be 5212IU/mg.
Activity Assay
More Info
-
Introduction
Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.
-
Synonyms
Chorionic gonadotropin, hCG, CG.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized hCG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CG-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 Human Chorionic Gonadotropin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Contaminants
Free of: HbsAg and antibodies to HIV and HCV.
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 :
GCHFR HumanDescription:
GTP Cyclohydrolase I Feedback Regulator Human Recombinant
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
Product # :
PRO-2006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.
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Synonyms
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
-
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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.
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 :
VPS29 MouseDescription:
Vacuolar Protein Sorting 29 Mouse Recombinant
Vacuolar protein sorting 29 yeast homolog (S. cerevisiae), DC15, PEP11, DC7, retromer protein, x 007 protein, EC 3.1.3.3.
Product # :
PRO-1066Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
VPS29 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-182) and having a molecular mass of 23.2kDa.VPS29 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The VPS29 solution (0.5mg/1ml) 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
VPS29 is a member of a group of genes coding for vacuolar protein sorting (VPS) proteins which, when functionally damaged, lessens the efficient transfer of vacuolar hydrolases. VPS29 is a late Golgi transmembrane protein that operates as the sorting receptor for soluble vacuolar hydrolases, from the prevacuolar endosome back to the Golgi. Moreover, VPS29 takes part in the creation of the inner shell of the retromer coat for retrograde vesicles parting the prevacuolar compartment.
-
Synonyms
Vacuolar protein sorting 29 yeast homolog (S. cerevisiae), DC15, PEP11, DC7, retromer protein, x 007 protein, EC 3.1.3.3.
-
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 MGSHMMLVLV LGDLHIPHRC NSLPAKFKKL LVPGKIQHIL CTGNLCTKES YDYLKTLAGD VHIVRGDFDE NLNYPEQKVV TVGQFKIGLI HGHQVIPWGD MASLALLQRQ FDVDILISGH THKFEAFEHE NKFYINPGSA TGAYNALETN IIPSFVLMDI QASTVVTYVY QLIGDDVKVE RIEYKKS
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 :
GDNF Human, Sf9Description:
Glial-Derived Neurotrophic Factor Human Recombinant, Sf9
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
Product # :
CYT-1162Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GDNF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.
-
Synonyms
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
-
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
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
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Background
What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.
What is the source or expression system of GDNF HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF HUMAN, SF9 Protein?
The biological functionality of GDNF HUMAN, SF9 Protein will be determined in the future.
What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
What applications can GDNF HUMAN, SF9 Protein be used in?
GDNF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF HUMAN, SF9 Protein?
The endotoxin level is minimal, GDNF HUMAN, SF9 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 :
SHBG ProteinDescription:
Sex Hormone-Binding Globulin Human
Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.
Product # :
PRO-2757Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- More Info
Description
SHBG is a protein of approximately 45kD.
Source
Human serum.
Formulation
The protein is supplied in 0.01M HEPES, PH 7.4 and 0.15M NaCl.
More Info
-
Introduction
Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, insulin and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.
-
Synonyms
Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.
-
Physical Appearance
Streile filtered colorless solution.
-
Stability
Upon arrival, Store at -20°C. Please prevent freeze-thaw cycles.
-
Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, Parvovirus B19, HBc, HBV, HIV and Syphilis.
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 :
BNP ProteinDescription:
B-type Natriuretic Peptide Human Recombinant
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
-
Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NPPB 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 B-type Natriuretic Peptide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
-
Background
What is the molecular weight / Mw of BNP Protein?
BNP Protein has a total Mw of 3.5kDa.
What is the source or expression system of BNP Protein?
Escherichia Coli.
What is the Purity of BNP Protein?
BNP Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BNP Protein?
The biological functionality of BNP Protein will be determined in the future.
What is the amino acid sequence of BNP Protein?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
What applications can BNP Protein Protein be used in?
BNP Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BNP Protein?
The endotoxin level is minimal, BNP 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 :
FGF17 HumanDescription:
Fibroblast Growth Factor 17 Human Recombinant
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
Product # :
CYT-817Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.
Source
Escherichia Coli.
Formulation
FGF17 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
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.More Info
-
Introduction
Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.
-
Synonyms
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF17 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.
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Solubility
It is recommended to reconstitute the lyophilized FGF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.
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Background
What is the molecular weight/Mw of FGF17 Protein?
FGF17 Protein has a total Mw of 22.6kDa.
What is the source or expression system of FGF17 Protein?
Escherichia Coli.
What is the Purity of FGF17 Protein?
FGF17 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF17 Protein?
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.
What is the amino acid sequence of FGF17 Protein?
MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.
What applications can FGF17 Protein be used in?
FGF17 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF17 Protein?
The endotoxin level is minimal, FGF17 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 :
LTF Human S.PlasmaDescription:
Lactoferrin Human (Seminal Plasma)
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Product # :
PRO-1591Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The Human Lactoferrin produced from pooled Human seminal plasma has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.
Source
Human seminal plasma.
Formulation
LTF protein filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Purity greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.
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Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK DKSPKFQLFG SPSGQKDLLF KDSAIGFSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALVLKGEAD AMSLDGGYVY TAGKCGLVPV LAENYKSQQS SDPDPNCVDR PVEGYLAVAV VRRSDTSLTW NSVKGKKSCH TAVDRTAGWN IPMGLLFNQT GSCKFDEYFS QSCAPGSDPR SNLCALCIGD EQGENKCVPN SNERYYGYTG AFRCLAENAG DVAFVKDVTV LQNTDGNNNE AWAKDLKLAD FALLCLDGKR KPVTEARSCH LAMAPNHAVV SRMDKVERLK QVLLHQQAKF GRNGSDCPDK FCLFQSETKN LLFNDNTECL ARLHGKTTYE KYLGPQYVAG ITNLKKCSTS PLLEACEFLR K.
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Human Virus Test
Samples from each donor have been tested and found negative for HBsAg, HIV-1+2, HCV, syphilis, aHBc, RRR.
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 :
VCAM1 Human, sf9Description:
Vascular cell adhesion molecule 1 Human Recombinant, sf9
Vascular Cell Adhesion Molecule 1, CD106 Antigen, INCAM-100 , Vascular Cell Adhesion Protein 1, V-CAM 1, VCAM-1, CD106, L1CAM.
Product # :
PRO-2367Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
VCAM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 685 amino acids (25-698 a.a.) and having a molecular mass of 75.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). VCAM1 is expressed with a 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
VCAM1 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.
More Info
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Introduction
VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).
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Synonyms
Vascular Cell Adhesion Molecule 1, CD106 Antigen, INCAM-100 , Vascular Cell Adhesion Protein 1, V-CAM 1, VCAM-1, CD106, L1CAM.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPEFFKIET TPESRYLAQI GDSVSLTCST TGCESPFFSW RTQIDSPLNG KVTNEGTTST LTMNPVSFGN EHSYLCTATC ESRKLEKGIQ VEIYSFPKDP EIHLSGPLEA GKPITVKCSV ADVYPFDRLE IDLLKGDHLM KSQEFLEDAD RKSLETKSLE VTFTPVIEDI GKVLVCRAKL HIDEMDSVPT VRQAVKELQV YISPKNTVIS VNPSTKLQEG GSVTMTCSSE GLPAPEIFWS KKLDNGNLQH LSGNATLTLI AMRMEDSGIY VCEGVNLIGK NRKEVELIVQ EKPFTVEISP GPRIAAQIGD SVMLTCSVMG CESPSFSWRT QIDSPLSGKV RSEGTNSTLT LSPVSFENEH SYLCTVTCGH KKLEKGIQVE LYSFPRDPEI EMSGGLVNGS SVTVSCKVPS VYPLDRLEIE LLKGETILEN IEFLEDTDMK SLENKSLEMT FIPTIEDTGK ALVCQAKLHI DDMEFEPKQR QSTQTLYVNV APRDTTVLVS PSSILEEGSS VNMTCLSQGF PAPKILWSRQ LPNGELQPLS ENATLTLIST KMEDSGVYLC EGINQAGRSR KEVELIIQVT PKDIKLTAFP SESVKEGDTV IISCTCGNVP ETWIILKKKA ETGDTVLKSI DGAYTIRKAQ LKDAGVYECE SKNKVGSQLR SLTLDVQGRE NNKDYFSPEH 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 :
EGFPDescription:
Enhanced Green Fluorescent Protein Recombinant
Green fluorescent protein, GFP.
Product # :
PRO-1606Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGFP 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.More Info
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Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
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Synonyms
Green fluorescent protein, GFP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK
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.