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Search results

1000 results found for “lactoferrin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    TNF a Rat, His

    Description:

    Tumor Necrosis Factor-alpha Rat Recombinant, His Tag

    Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    Product # :

    CYT-900

    Price :

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    • description
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    Description

    TNF a Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235a.a.) and having a molecular mass of 19.9kDa.TNF a is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF a protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.

    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.

    Tnf A Rat His
  • View Data Sheet

    Name :

    CST7 Human

    Description:

    Cystatin 7 Human Recombinant

    Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

    Product # :

    PRO-2222

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    Description

    CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CST7 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.

    • Synonyms

      Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cst7 Human
  • View Data Sheet

    Name :

    MLEC Human

    Description:

    Malectin Human Recombinant

    Malectin, KIAA0152, Oligosaccharyltransferase Complex Subunit (Non-Catalytic).

    Product # :

    PRO-1614

    Price :

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    • description
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    Description

    MLEC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (29-269) and having a molecular mass of 29.1kDa.MLEC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MLEC solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MLEC is a member of the malectin family and is found on endoplasmic reticulum membrane. MLEC is a carbohydrate-binding protein with a high ligand preference for Glc2-N-glycan. MLEC takes part in the initial stages of protein N-glycosylation.

    • Synonyms

      Malectin, KIAA0152, Oligosaccharyltransferase Complex Subunit (Non-Catalytic).

    • 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 MGSPGLGVAG VAGAAGAGLP ESVIWAVNAG GEAHVDVHGI HFRKDPLEGR VGRASDYGMK LPILRSNPED QILYQTERYN EETFGYEVPI KEEGDYVLVL KFAEVYFAQS QQKVFDVRLN GHVVVKDLDI FDRVGHSTAH DEIIPMSIRK GKLSVQGEVS TFTGKLYIEF VKGYYDNPKV CALYIMAGTV DDVPKLQPHP GLEKKEEEEE EEEYDEGSNL KKQTNKNRVQ SGPRTPNPYA SDNS

    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.

    Mlec Human
  • View Data Sheet

    Name :

    AFP Protein

    Description:

    Alpha Fetoprotein Human Recombinant

    Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.

    Product # :

    PRO-2229

    Price :

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    • description
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    Description

    AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 600 amino acids (19-609a.a.) and having a molecular mass of 67.5kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). AFP is expressed with a ADP at N-terminus and 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    AFP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.

    • Synonyms

      Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.

    • 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

      ADPRTLHRNEYGI ASILDSYQCT AEISLADLAT IFFAQFVQEA TYKEVSKMVK DALTAIEKPT GDEQSSGCLE NQLPAFLEEL CHEKEILEKY GHSDCCSQSE EGRHNCFLAH KKPTPASIPL FQVPEPVTSC EAYEEDRETF MNKFIYEIAR RHPFLYAPTI LLWAARYDKI IPSCCKAENA VECFQTKAAT VTKELRESSL LNQHACAVMK NFGTRTFQAI TVTKLSQKFT KVNFTEIQKL VLDVAHVHEH CCRGDVLDCL QDGEKIMSYI CSQQDTLSNK ITECCKLTTL ERGQCIIHAE NDEKPEGLSP NLNRFLGDRD FNQFSSGEKN IFLASFVHEY SRRHPQLAVS VILRVAKGYQ ELLEKCFQTE NPLECQDKGE EELQKYIQES QALAKRSCGL FQKLGEYYLQ NAFLVAYTKK APQLTSSELM AITRKMAATA ATCCQLSEDK LLACGEGAAD IIIGHLCIRH EMTPVNPGVG QCCTSSYANR RPCFSSLVVD ETYVPPAFSD DKFIFHKDLC QAQGVALQTM KQEFLINLVK QKPQITEEQL EAVIADFSGL LEKCCQGQEQ EVCFAEEGQK LISKTRAALG VHHHHHH.

    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.

    Afp Human
  • View Data Sheet

    Name :

    NCF1 Human

    Description:

    Neutrophil Cytosolic Factor 1 Human Recombinant

    NCF1A, NOXO2, p47phox, SH3PXD1A .

    Product # :

    PRO-488

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    Description

    NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
      Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.

    • Synonyms

      NCF1A, NOXO2, p47phox, SH3PXD1A .

    • 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

      MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

    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.

    Ncf1 Human
  • View Data Sheet

    Name :

    APOD Human, HEK

    Description:

    Apolipoprotein-D Human Recombinant, HEK

    Apolipoprotein D, Apo-D, ApoD.

    Product # :

    CYT-768

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    Description

    Apolipoprotein-D Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 21-189) containing a total of 175 amino acids, having a molecular mass of 20.1kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human APOD is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
      Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue.

    • Synonyms

      Apolipoprotein D, Apo-D, ApoD.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add deionized water to a working concentration of 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.

    • Amino Acid Sequence

      QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.

    • Background

      What is the molecular weight/Mw of APO D Protein?
      APO D Protein has a total Mw of 20.1kDa.

      What is the source or expression system of APO D Protein?
      HEK 293.

      What is the Purity of APO D Protein?
      APO D Protein is >80% pure as determined by SDS-PAGE.

      What is the Biological Activity of APO D Protein?
      The biological functionality of APO D Protein will be determined in the future.

      What is the amino acid sequence of APO D Protein?
      QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.

      What applications can APO D Protein be used in?
      APO D Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APO D Protein?
      The endotoxin level is minimal, APO D 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.

    Apod Human Hek
  • View Data Sheet

    Name :

    APOM Human, HEK

    Description:

    Apolipoprotein-M Human Recombinant, HEK

    G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

    Product # :

    CYT-026

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    Description

    APOM HEK Human Recombinant Protein is 20 kDa protein containing 179 amino acid residues of the APOM Human and 13 additional amino acid residues of flag Tag.

    Source

    HEK293.

    Formulation

    APOM Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport.

    • Synonyms

      G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized APOM Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted APOM Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN

    • Applications

      Cell culture and/or animal studies, ELISA and Western blotting.

    • Background

      What is the molecular weight/Mw of APOM Protein?
      APOM Protein has a total Mw of 20kDa.

      What is the source or expression system of APOM Protein?
      HEK293.

      What is the Purity of APOM Protein?
      APOM Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOM Protein?
      The biological functionality of APOM Protein will be determined in the future.

      What is the amino acid sequence of APOM Protein?
      HVDYKDDDDK PAGCPEHSQL TTLGVDGKEF PEVHLGQWYF IAGAAPTKEE LATFDPVDNI VFNMAAGSAP MQLHLRATIR MKDGLCVPRK WIYHLTEGST DLRTEGRPDM KTELFSSSCP GGIMLNETGQ GYQRFLLYNR SPHPPEKCVE EFKSLTSCLD SKAFLLTPRN QEACELSNN

      What applications can APOM Protein be used in?
      APOM Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOM Protein?
      The endotoxin level is minimal, APOM 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.

    Apom Human Hek
  • View Data Sheet

    Name :

    SOST Human, HEK

    Description:

    Sclerostin Human Recombinant, HEK

    Sclerostin, SOST, CDD, VBCH.

    Product # :

    PRO-2481

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    Description

    SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).

    Source

    HEK293 Cells.

    Formulation

    SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      Sclerostin, SOST, CDD, VBCH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY HHHHHH.

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    Sost Protein
  • View Data Sheet

    Name :

    SOST Mouse

    Description:

    Sclerostin Mouse Recombinant

    SOST, Sclerostin, 5430411E23Rik.

    Product # :

    PRO-2670

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    Description

    SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SOST 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

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      SOST, Sclerostin, 5430411E23Rik.

    • 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

      QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH HHHH

    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.

    Sclerostin Mouse
  • View Data Sheet

    Name :

    BST1 Human

    Description:

    Bone Marrow Stromal Cell Antigen 1 Human Recombinant

    Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

    Product # :

    CYT-1071

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    Description

    BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.

    • Synonyms

      Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

    • Background

      The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine

      Introduction

      In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.

      BST-1: A Versatile Player

      BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.

      Engineering a Cellular Conductor

      With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.

      Entering the Biological Stage

      Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.

      An Enthusiastic Applause for Results

      Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.

      Conclusion

      The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.

      What is the molecular weight/Mw of BST1 Protein?
      BST1 Protein has a total Mw of 30.5kDa.

      What is the source or expression system of BST1 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of BST1 Protein?
      BST1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BST1 Protein?
      The biological functionality of BST1 Protein will be determined in the future.

      What is the amino acid sequence of BST1 Protein?
      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

      What applications can BST1 Protein be used in?
      BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BST1 Protein?
      The endotoxin level is minimal, BST1 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Bst1 Human
  • View Data Sheet

    Name :

    IL 7 Human, Yeast

    Description:

    Interleukin-7 Human Recombinant, Yeast

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-298

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    Description

    Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 Interleukin -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.418 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). 2. Analysis by RP-HPLC, using a standard solution of IL-7 as a Reference Standard.

    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.

    Il 7 Human Yeast
  • View Data Sheet

    Name :

    FAM3A Human

    Description:

    Family with Sequence Similarity 3, Member A Human Recombinant

    Protein FAM3A, Cytokine-like protein 2-19, FAM3A, 2-19, 2.19, DLD, XAP-7, DXS560S.

    Product # :

    PRO-1584

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    Description

    FAM3A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 23.1kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    FAM3A filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Family with Sequence Similarity 3, Member A (FAM3A) is a member of the FAM3 family along with FAM3B (Pander) protein which induces apoptosis of pancreatic alpha and beta cells. FAM3A is a cytokine-like protein, which is expressed in almost all tissues such as the testis, pancreas, adrenal, placenta, brain, fetal brain, liver, kidney, skeletal muscle and the heart. FAM3A gene expression may be regulated by peroxisome proliferator-activated receptor gamma, and the FAM3A protein might be involved in the regulation of glucose and lipid metabolism. Although the function of the FAM3A protein has been unclear until now, it may act as a defensin against invading fungal microorganisms.

    • Synonyms

      Protein FAM3A, Cytokine-like protein 2-19, FAM3A, 2-19, 2.19, DLD, XAP-7, DXS560S.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FAM3A is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASFPRIQQLFTS PESSVTAAPR ARKYKCGLPQ PCPEEHLAFR VVSGAANVIG PKICLEDKML MSSVKDNVGR GLNIALVNGV SGELIEARAF DMWAGDVNDL LKFIRPLHEG TLVFVASYDD PATKMNEETR KLFSELGSRN AKELAFRDSW VFVGAKGVQN KSPFEQHVKN SKHSNKYEGW PEALEMEGCI PRRSTAS.

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    Fam3A Human
  • View Data Sheet

    Name :

    C1QTNF2 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 2 Human Recombinant

    Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.

    Product # :

    PRO-133

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    Description

    C1QTNF2 Protein is a 29,640 Da protein containing 280 aa fused to a 10 aa N-Terminal His-tag.

    Source

    E. coli

    Formulation

    C1QTNF2 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.03M Acetate buffer, pH 4.

    More Info

    • Introduction

      C1QTNF2 can be found in many different organism parts such as the testis, cervix. C1QTNF2 is located in the extracellular space and has various roles such as activation of MAPK activity, positive regulation of fatty acid oxidation, positive regulation of glycogen biosynthetic process, and positive regulation of glucose import.

    • Synonyms

      Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.

    • Stability

      Store lyophilized C1QTNF2 uman at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF2 an be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10?g/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG RTGNRGKPGP KGKAGAIGRA GPRGPKGVNG TPGKHGTPGK KGPKGKKGEP GLPGPCSCGS GHTKSAFSVA VTKSYPRERL PIKFDKILMN EGGHYNASSG KFVCGVPGIY YFTYDITLAN KHLAIGLVHN GQYRIRTFDA NTGNHDVASG STILALKQGD EVWLQIFYSE QNGLFYDPYW TDSLFTGFLI YADQDDPNEV.

    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.

    C1Qtnf2 Human
  • View Data Sheet

    Name :

    C1QTNF5 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 5 Human Recombinant

    CTRP5, MFRP.

    Product # :

    PRO-2599

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    Description

    C1QTNF5 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (16-243.a.a) and having a molecular mass of 26.4kDa. C1QTNF5 Human is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C1QTNF5 protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.5) containing 30% glycerol and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement C1q Tumor Necrosis Factor-Related Protein 5 (C1QTNF5) encodes a short-chain collagen which is expressed mainly in sub-retinal pigment epithelium, ciliary epithelium and adipose tissue. C1QTNF5 is increased in mtDNA-depleted myocytes and stimulates the phosphorylation of AMP activated protein kinase. C1QTNF5 takespart in the adhesion of the retinal pigment epithelium (RPE) to the Bruch Membrane. Mutations in C1QTNF5 have been associated with late-onset retinal degeneration.

    • Synonyms

      CTRP5, MFRP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMSPPLD DNKIPSLCPG HPGLPGTPGH HGSQGLPGRD
      GRDGRDGAPG APGEKGEGGR PGLPGPRGDP GPRGEAGPAG PTGPAGECSV PPRSAFSAKR
      SESRVPPPSD APLPFDRVLV NEQGHYDAVT GKFTCQVPGV YYFAVHATVY RASLQFDLVK
      NGESIASFFQ FFGGWPKPAS LSGGAMVRLE PEDQVWVQVG VGDYIGIYAS IKTDSTFSGF LVYSDWHSSP VFA.

    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.

    C1Qtnf5 Human
  • View Data Sheet

    Name :

    IL18BP Human, Sf9

    Description:

    Interleukin-18 Binding Protein Human Recombinant, Sf9

    Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.

    Product # :

    CYT-878

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    Description

    IL18BP Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 406 amino acids (31-194a.a) and having a molecular mass of 44.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). IL18BP is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL18BP protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.

    • Synonyms

      Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.

    • 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

      ADPTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQGLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il18Bp Human Sf9
  • View Data Sheet

    Name :

    TFF3 Rat

    Description:

    Trefoil Factor-3 Rat Recombinant

    Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.

    Product # :

    CYT-781

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    Description

    The Trefoil Factor-3 Rat was constructed as a recombinant protein with a 9 a.a C-terminal fusion of Flag-Tag (1 aa N-terminal+8 aa C-terminal). The TFF3 Rat produced in E.coli, is 7.7kDa protein containing a total of 68 amino acid residues.

    Source

    Escherichia Coli.

    Formulation

    TFF3 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.

    • Synonyms

      Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 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.

    • Amino Acid Sequence

      MQEFVGLSPS QCMVPANVRV DCGYPTVTSE QCNNRGCCFD SSIPNVPWCF KPLQETECT F DYKDDDDK.

    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.

    Tff3 Rat
  • View Data Sheet

    Name :

    CX3CL1 Human, His

    Description:

    Fractalkine Human Recombinant (CX3CL1), His Tag

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-360

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    • SDS-PAGE

    Description

    Fractalkine Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
      CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 HUMAN, HIS Protein?
      CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
      The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

      What applications can CX3CL1 HUMAN, HIS Protein be used in?
      CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.


    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.

    Fractalkine Human His
  • View Data Sheet

    Name :

    Follistatin Human, Sf9

    Description:

    Follistatin Human Recombinant, Sf9

    Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.

    Product # :

    CYT-865

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    • sds-page

    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

    Follistatin Human, Sf9-sds-page - Product image 1

    More Info

    • 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).

    • Synonyms

      Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.

    • 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

      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

    • 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.

    Fst Human Sf9
  • View Data Sheet

    Name :

    GADD45GIP1 Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

    Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    Product # :

    PRO-972

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    Description

    GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

    • Synonyms

      Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    • 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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

    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.

    Gadd45Gip1 Human
  • View Data Sheet

    Name :

    TOLLIP Human

    Description:

    Toll Interacting Protein 1 Human Recombinant

    Toll-interacting protein, TOLLIP, IL-1RAcPIP.

    Product # :

    PRO-228

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    Description

    TOLLIP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-274 a.a) and having a molecular mass of 32.4kDa.TOLLIP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TOLLIP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Toll interacting protein (TOLLIP) is an inhibitory adaptor protein within Toll-like receptors. The TLR pathway is a part of the innate immune system which recognizes structurally conserved molecular patterns of microbial pathogens, initiating an inflammatory immune response. Negative regulation of TLR signaling by TOLLIP might restrict the production of proinflammatory mediators during inflammation and infection. Furthermore, TOLLIP forms a complex with Tom1 to regulate endosomal transferring of ubiquitinated proteins.

    • Synonyms

      Toll-interacting protein, TOLLIP, IL-1RAcPIP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      TOLLIP Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MATTVSTQRG PVYIGELPQD FLRITPTQQQ RQVQLDAQAA QQLQYGGAVG TVGRLNITVV QAKLAKNYGM TRMDPYCRLR LGYAVYETPT AHNGAKNPRW NKVIHCTVPP GVDSFYLEIF DERAFSMDDR IAWTHITIPE SLRQGKVEDK WYSLSGRQGD DKEGMINLVM SYALLPAAMV MPPQPVVLMP TVYQQGVGYV PITGMPAVCS PGMVPVALPP AAVNAQPRCS EEDLKAIQDM FPNMDQEVIR SVLEAQRGNK DAAINSLLQM GEEP.

    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.

    Tollip Human
  • View Data Sheet

    Name :

    Pro-IGF2 Human

    Description:

    Pro-Insulin Like Growth Factor-2 Human Recombinant

    Pro-Insulin Like Growth Factor-2, pro-IGF2.

    Product # :

    CYT-110

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    Description

    Pro-IGF2 Human Recombinant produced in HEK cells is a glycosylated monomer, contains 157 a.a. (24-180) having a total molecular weight of 25kDa.The Pro-IGF2 contains a C-terminal propeptide (E peptide) Arg92 to Lys180 and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The Pro-IGF2 was lyophilized in 50mM Sodium Acetate pH 4.5 and 350mM NaCl.

    Purity

    Greater than 90% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of MCF-7 cells (human breast cancer cell line) and is typically 2-8ng/ml.

    More Info

    • Introduction

      IGF-2 is a member of the insulin family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3' region and to the upstream INS gene at the 5' region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Pro-Insulin Like Growth Factor-2, pro-IGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pro-IGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pro-IGF2 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 Pro-IGF2 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Background

      What is the molecular weight/Mw of PRO-IGF2 HUMAN Protein?
      PRO-IGF2 HUMAN Protein has a total Mw of 25kDa.

      What is the source or expression system of PRO-IGF2 HUMAN Protein?
      HEK.

      What is the Purity of PRO-IGF2 HUMAN Protein?
      PRO-IGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of PRO-IGF2 HUMAN Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of MCF-7 cells (human breast cancer cell line) and is typically 2-8ng/ml.

      What applications can PRO-IGF2 HUMAN Protein be used in?
      PRO-IGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for PRO-IGF2 HUMAN Protein?
      The endotoxin level is minimal, PRO-IGF2 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.

    Pro Igf2 Human
  • View Data Sheet

    Name :

    L-Selectin Human, Sf9

    Description:

    L-Selectin Human Recombinant, Sf9

    Selectin L, Leukocyte-Endothelial Cell Adhesion Molecule 1, CD62 Antigen-Like Family Member L, Leukocyte Surface Antigen Leu-8, Lymphocyte Adhesion Molecule 1, Lymph Node Homing Receptor, Gp90-MEL, LECAM1, LYAM1, LNHR, TQ1, Leukocyte Adhesion Molecule, Pln Homing Receptor, CD62L Antigen, L-Selectin, CD62L, PLNHR, LAM-1, LAM1, LEU8, LSEL, L-selectin.

    Product # :

    PRO-2487

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    Description

    L-Selectin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 303 amino acids (52-345a.a.) and having a molecular mass of 34.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).L-Selectin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    L-Selectin protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
      L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
      L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

    • Synonyms

      Selectin L, Leukocyte-Endothelial Cell Adhesion Molecule 1, CD62 Antigen-Like Family Member L, Leukocyte Surface Antigen Leu-8, Lymphocyte Adhesion Molecule 1, Lymph Node Homing Receptor, Gp90-MEL, LECAM1, LYAM1, LNHR, TQ1, Leukocyte Adhesion Molecule, Pln Homing Receptor, CD62L Antigen, L-Selectin, CD62L, PLNHR, LAM-1, LAM1, LEU8, LSEL, L-selectin.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPWTYHYSE KPMNWQRARR FCRDNYTDLV AIQNKAEIEY LEKTLPFSRS YYWIGIRKIG GIWTWVGTNK SLTEEAENWG DGEPNNKKNK EDCVEIYIKR NKDAGKWNDD ACHKLKAALC YTASCQPWSC SGHGECVEII NNYTCNCDVG YYGPQCQFVI QCEPLEAPEL GTMDCTHPLG NFSFSSQCAF SCSEGTNLTG IEETTCGPFG NWSSPEPTCQ VIQCEPLSAP DLGIMNCSHP LASFSFTSAC TFICSEGTEL IGKKKTICES SGIWSNPSPI CQKLDKSFSM IKEGDYNHHH HHH.

    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.

    L Selectin
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    Name :

    CIDEC Human

    Description:

    Cell Death-Inducing DFFA-Like Effector C Human Recombinant

    Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    Product # :

    PRO-2026

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    Description

    CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.

    Source

    Escherichia Coli.

    Formulation

    CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.

    • Synonyms

      Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    • Physical Appearance

      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

      MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.

    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.

    Cidec Human
  • View Data Sheet

    Name :

    ULBP3 Human

    Description:

    UL16 Binding Protein 3 Human Recombinant

    UL16 Binding Protein 3, Retinoic Acid Early Transcript 1N, ALCAN-Gamma, NKG2DL3, N2DL-3, RAET1N, UL16-Binding Protein 3, NKG2D Ligand 3, N2DL3, ULBP3.

    Product # :

    PRO-2039

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    Description

    ULBP3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Asp30-Gly217) containing 198 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 23.25kDa.

    Source

    Escherichia Coli.

    Formulation

    ULBP3 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 0.1% v/v amisoft CS-22, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      UL16 Binding Protein 3 (ULBP3) is a ligand for the NKG2D receptor in NK cells. ULBPs activate different signaling pathways resulting in the production of cytokines and chemokines. ULBP3 is a ligand for the KLRK1/NKG2D receptor, along with at least ULBP1 and ULBP2. Binding of ULBPs ligands to KLRK1/NKG2D stimulates calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. ULBP3 has lower affinity for KLRK1/NKG2D compared to ULBP1 and ULBP2 and stimulates weaker signaling responses than does ULBP2 or ULBP1.

    • Synonyms

      UL16 Binding Protein 3, Retinoic Acid Early Transcript 1N, ALCAN-Gamma, NKG2DL3, N2DL-3, RAET1N, UL16-Binding Protein 3, NKG2D Ligand 3, N2DL3, ULBP3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ULBP3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASDAHSLWYNFT IIHLPRHGQQ WCEVQSQVDQ KNFLSYDCGS DKVLSMGHLE EQLYATDAWG KQLEMLREVG QRLRLELADT ELEDFTPSGP LTLQVRMSCE CEADGYIRGS WQFSFDGRKF LLFDSNNRKW TVVHAGARRM KEKWEKDSGL TTFFKMVSMR DCKSWLRDFL MHRKKRLEPT APPTMAPG.

    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.

    Ulbp3 Human
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