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Name :
Myostatin Propeptide HumanDescription:
Myostatin Propeptide Human Recombinant
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-448Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.
Source
Escherichia Coli.
Formulation
Lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.Citations
More Info
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Introduction
Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
Sterile 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.
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Solubility
It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.
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 :
PRDX2 MouseDescription:
Eukaryotic Translation Initiation Factor 4E Mouse Recombinant
PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.
Product # :
ENZ-1061Price :
Quantity :
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Shipped with Ice Packs
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Description
PRDX2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PRDX2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700 pmol/min/ug, Activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for minute.
Citations
More Info
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Introduction
PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer. -
Synonyms
PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASGNA QIGKSAPDFT ATAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN
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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
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Shipped with Ice Packs
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TBCA HumanDescription:
Tubulin Folding Cofactor A Human Recombinant
Tubulin-specific chaperone A, Tubulin-folding cofactor A, CFA, TCP1-chaperonin cofactor A, TBCA.
Product # :
PRO-705Price :
Quantity :
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Shipped with Ice Packs
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Description
TBCA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids (1-108 a.a.) and having a molecular mass of 12.8 kDa.The TBCA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TBCA solution contains 20mM Tris-HCl buffer pH 7.5, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TBCA is a tubulin-folding protein which is involved in the early step of the tubulin folding pathway. TBCA is one of four proteins (cofactors A, D, E, and C) implicated in the pathway directing to properly folded beta-tubulin from folding intermediates. Cofactors A and D are thought to be a factor in capturing and stabilizing beta-tubulin in a quasi-native confirmation. TBCA is crucial for cell viability, if reduced it causes a decrease in the amount of soluble tubulin, alterations in microtubules and G1 cell cycle arrest. Cofactor E attaches to the cofactor D-tubulin complex, afterward, interaction with cofactor C triggers the release of tubulin polypeptides that are committed to the native state.
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Synonyms
Tubulin-specific chaperone A, Tubulin-folding cofactor A, CFA, TCP1-chaperonin cofactor A, TBCA.
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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
MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQAEILQES RMMIPDCQRR LEAAYLDLQR ILENEKDLEE AEEYKEARLV LDSVKLEA.
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 :
Follistatin Human, Sf9Description:
Follistatin Human Recombinant, Sf9
Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.
Product # :
CYT-865Price :
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Description
FST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (30-317a.a.) and having a molecular mass of 32.5kDa.FST is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FST protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.
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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
MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, SF9 Protein?
FOLLISTATIN HUMAN, SF9 Protein has a total Mw of 32.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of FOLLISTATIN HUMAN, SF9 Protein?
FOLLISTATIN HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN, SF9 Protein?
The biological functionality of FOLLISTATIN HUMAN, SF9 Protein will be determined in the future.
What is the amino acid sequence of FOLLISTATIN HUMAN, SF9 Protein?
MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH.
What applications can FOLLISTATIN HUMAN, SF9 Protein be used in?
FOLLISTATIN HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN, SF9 Protein?
The endotoxin level is minimal, FOLLISTATIN 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.
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Name :
PCSK1N HumanDescription:
Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant
ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.
Product # :
PRO-1819Price :
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Shipped with Ice Packs
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Description
PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.
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Synonyms
ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.
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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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.
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 :
DCN HumanDescription:
Decorin Human Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
Product # :
PRO-1583Price :
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Shipped with Ice Packs
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Description
DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
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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 MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.
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 :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
Quantity :
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Shipped with Ice Packs
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
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Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
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 :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
Citations
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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 :
GH HumanDescription:
Growth Hormone Human Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-202Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22kDa. Growth Hormone is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GH protein lyophilized from a 0.2µm filtered concentrated solution containing mannitol, and glycine.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation assay of rat lymphoma NB2-11 cells and was found to be less than 0.1ng/ml.
Citations
More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four 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 is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five 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 four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGH 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 HGH 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
FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS LVYGASDSNV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F.
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 :
PHLDA2 HumanDescription:
Pleckstrin homology-like domain family A member 2 Human Recombinant
Pleckstrin homology-like domain family A member 2, Imprinted in placenta and liver protein, Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein, Tumor-suppressing STF cDNA 3 protein, Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein, p17-Beckwith-Wiedemann region 1 C, PHLDA2, BWR1C, HLDA2, IPL, TSSC3, BRW1C.
Product # :
PRO-781Price :
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Description
PHLDA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids (1-152 a.a.) and having a molecular mass of 19.2 kDa. PHLDA2 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PHLDA2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Pleckstrin homology-like domain family A member 2 (PHLDA2) is a cytoplasmic protein, which is involved in fetal and placental growth. PHLDA2 is an apoptosis-related protein, which acts as a negative growth regulator and is expressed during normal human development. PHLDA2 is imprinted on placenta, liver and fetal tissues during embryogenesis and is removed once development is complete. The PHLDA2 gene is one of a number of genes in the imprinted gene domain of 11p15.5 which is considered to be an important tumor suppressor gene region. Changes in this region may be linked to the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. PHLDA2 is expressed in placenta (present in all cells of the villous cytotrophoblast) and adult prostate gland. Furthermore, PHLDA2 is expressed in adult brain and neuroblastoma, medullablastoma and glioblastoma cell lines and at low levels in adult liver and lung, and fetal liver.
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Synonyms
Pleckstrin homology-like domain family A member 2, Imprinted in placenta and liver protein, Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein, Tumor-suppressing STF cDNA 3 protein, Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein, p17-Beckwith-Wiedemann region 1 C, PHLDA2, BWR1C, HLDA2, IPL, TSSC3, BRW1C.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
PHLDA2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKSPDEVLRE GELEKRSDSL FQLWKKKRGV LTSDRLSLFP ASPRARPKEL RFHSILKVDC VERTGKYVYF TIVTTDHKEI DFRCAGESCW NAAIALALID FQNRRALQDF RSRQERTAPA APAEDAVAAA AAAPSEPSEP SRPSPQPKPR TP.
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 :
CTSD HumanDescription:
Cathepsin-D Human Recombinant
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
Product # :
ENZ-378Price :
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Description
CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells
Formulation
CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE
Citations
More Info
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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
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Synonyms
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Amino Acid Sequence
LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH
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Enzymatic Activity
> 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.
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 :
TIPIN HumanDescription:
TIMELESS Interacting Protein Human Recombinant
TIMELESS Interacting Protein, CSM3 Homolog.
Product # :
PRO-1710Price :
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Description
TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.
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Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR
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 :
Prolactin OvineDescription:
Prolactin Ovine Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-240Price :
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Shipped at Room temp
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Description
Prolactin Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23 kDa. The Prolactin n is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Is fully biologically active as evidenced by inducing proliferation of Nb2 cells.Citations
More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prl 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 Prolactin in sterile 18MΩ-cm H2O or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Thr-Pro-Val-Cys-Pro.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC DNAman computer 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.
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Name :
UFM1 HumanDescription:
Ubiquitin-Fold Modifier 1 Human Recombinant
Ubiquitin-fold modifier 1, UFM1, C13orf20, BM-002, bA131P10.1.
Product # :
PRO-125Price :
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Description
UFM1 Human Recombinant fused with a20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing103 amino acids (1-83 a.a) and having a molecular mass of 11.1kDa. The UFM1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UFM1 solution (1 mg/ml) 20mM Tris buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
UFM1 is a ubiquitin-like protein which is conjugated to target proteins by E1-like activating enzyme UBA5 and E2-like conjugating enzyme UFC1 in a manner equivalent to ubiquitylation. UFM1 localizes principally to the nucleus, but is also present in diffuse amounts in the cytoplasm. UFM1 is expressed in a variety of tissues, including kidney, brain, heart, liver and lung.
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Synonyms
Ubiquitin-fold modifier 1, UFM1, C13orf20, BM-002, bA131P10.1.
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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 MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA QTAGNVFLKH GSELRIIPRD RVG.
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 :
PIP ProteinDescription:
Prolactin-Induced Protein Human Recombinant
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
Product # :
CYT-793Price :
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Description
PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIP protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.
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Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.
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 :
WNV Pre-MDescription:
West Nile Virus Pre-M Recombinant
Product # :
WNV-002Price :
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Description
The E.Coli derived 20kda recombinant protein contains the West-Nile N-Terminal Pre-M Virus immunodominant regions. The protein is fused with 6xHis tag at c-terminal.
Source
Escherichia Coli.
Formulation
20mM phosphate buffer pH 7.5.
Purity
Protein is >95% pure as determined by SDS-PAGE.
Citations
More Info
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Introduction
West Nile virus (WNV) is a virus of the family Flaviviridae part of the Japanese encephalitis (JE) antigenic complex of viruses. Image reconstructions and cryoelectron microscopyreveal a 45-50 nm virion covered with a relatively smooth proteinsurface. This structure is similar to virus; both belong to the genus flavivirus within the family Flaviviridae. WNV is a positive-sense, single strand of RNA, it is between 11,000 and 12,000 nucleotides long which encode seven non-structural proteins and three structural proteins. The RNA strand is held within a nucleocapsid formed from 12 kDaprotein blocks; the capsid is contained within a host-derived membrane altered by two viral glycoproteins.
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Stability
WNV Pre-M although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRA MDVGYLCEDTITYECPVLAAGNDPEDIDCWCTKSSVYVR
YGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTK
ATRYLVKTESWILRNPGYALE. -
Applications
Antigen in ELISA and Western blots, excellent antigen for detection of West-Nile virus with minimal specificity problems.
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Specificity
Immunoreactive with sera of West Nile virus infected individuals.
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Purification Method
Purified by proprietary chromatographic technique.
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 :
Prolactin Mouse, PEGDescription:
Prolactin Pegylated Mouse Recombinant
Product # :
CYT-1247Price :
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Description
Pegylated Prolactin Mouse Recombinant is a single non-glycosilated polypeptide chain having a molecular mass of ~ 39 kDa containing 199 amino acids and an additional Ala at N-terminus Prolactin Mouse was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Mouse Prolactin inhibits proliferation of Nb2 cells or Baf/3 cells stably transfected with human prolactin receptors, though its activity is lower than pegylated human prolactin. However, it is anticipated that its activity in vivo in mice will be higher due to prolonged persistence in circulation.
Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin Mouse although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization Prolactin mouse can be stored at 4°C for several weeks. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Prolactin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Prolactin aka as lactotropin and mammotropin, is a neuroendocrine hormone synthesized primarily by the pituitary gland in response to eating but also a variety of other cell types including the placenta, brain and uterus. Prolactin takes part in metabolism, regulation of the immune system and pancreatic development. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.675 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by DNAman computer 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.
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Name :
Prolactin Ovine, HisDescription:
Ovine Prolactin Recombinant, His Tag
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1185Price :
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Description
Prolactin Ovine produced in E.Coli is a single, non-glycosylated polypeptide chain, fused to a 6 His Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
(1mg/ml) in 1 X PBS, pH 7.2 and 50% glycerol.
Purity
Protein is >90% pure as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Prolactin’s primary function is to promote and maintain lactation and also in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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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.
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 :
Follistatin MouseDescription:
Follistatin Mouse Recombinant
Follistatin, FST, FS, Activin-binding protein, AL033346.
Product # :
CYT-124Price :
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Description
Follistatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids and having a total molecular mass of 31.6kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse Follistatin is lyophilized from 10mM Na2PO4 and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.Citations
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
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Background
What is the molecular weight/Mw of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein has a total Mw of 31.6kDa.
What is the source or expression system of FOLLISTATIN MOUSE Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN MOUSE Protein?
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.
What is the amino acid sequence of FOLLISTATIN MOUSE Protein?
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
What applications can FOLLISTATIN MOUSE Protein be used in?
FOLLISTATIN MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN MOUSE Protein?
The endotoxin level is minimal, FOLLISTATIN MOUSE 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 :
LCN1 HumanDescription:
Lipocalin-1 Human Recombinant
Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.
Product # :
ENZ-825Price :
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Shipped with Ice Packs
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Description
LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.
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Synonyms
Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.
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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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.
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 :
Hemopexin HumanDescription:
Hemopexin Human Recombinant
Hemopexin, Beta-1B-glycoprotein, HPX, Haemopexin.
Product # :
PRO-1869Price :
Quantity :
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Description
Hemopexin Human Recombinant produced in E. coli is. a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 51.7kDa. Hemopexin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Hemopexin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid
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Synonyms
Hemopexin, Beta-1B-glycoprotein, HPX, Haemopexin.
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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 MGSTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH.
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 :
Leptin PufferfishDescription:
Leptin Pufferfish Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-530Price :
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Description
Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.Citations
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
ARPC5 HumanDescription:
Actin Related Protein 2/3 Complex, Subunit 5 Human Recombinant
Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.
Product # :
PRO-145Price :
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Shipping Method :
Shipped with Ice Packs
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Description
ARPC5 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 18.4kDa. The ARPC5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARPC5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ARPC5 is a 151 amino acid subunit of the Arp2/3 complex. ARPC5 is believed to have a role in maintaining the integrity of Arp2/3. ARPC5 is a substrate for MAPKAPK-2 which, via phosphorylation of ARPC5, may participate in Arp2/3 regulatory functions and remodeling of the Actin cytoskeleton.
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Synonyms
Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.
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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 MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN SSAMLLQWHE KALAAGGVGS IVRVLTARKT V.
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.