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  • View Data Sheet

    Description:

    Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

    IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

    Product # :

    CYT-1138

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    • SDS-PAGE

    Description

    IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.

    • Synonyms

      IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

    • Background

      What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.

      What is the source or expression system of IFNAR1 HUMAN Protein?
      Sf9, Insect cells.

      What is the Purity of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR1 HUMAN Protein?
      The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IFNAR1 HUMAN Protein?
      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

      What applications can IFNAR1 HUMAN Protein be used in?
      IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR1 HUMAN Protein?
      The endotoxin level is minimal, IFNAR1 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.

    Ifnar1 Human
  • View Data Sheet

    Description:

    Interleukin-22 Human Recombinant, Sf9

    IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

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    CYT-1092

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    Description

    IL22 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (34-179 a.a.) fused to a 6 aa His Tag at C-terminus containing a total of 155 amino acids and having a molecular mass of 17.8kDa. IL22 is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL22 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to induce IL-10 secretion using COLO 205 human colorectal adenocarcinoma cell is ≤ 1.2 ng/ml.

    More Info

    • Introduction

      Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R? (previously known as CRF2-4), belonging to the class II cytokine receptor family.

    • Synonyms

      IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    • 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

      ADPAPISSHC RLDKSNFQQP YITNRTFMLA KEASLADNNT DVRLIGEKLF HGVSMSERCY LMKQVLNFTL EEVLFPQSDR FQPYMQEVVP FLARLSNRLS TCHIEGDDLH IQRNVQKLKD TVKKLGESGE IKAIGELDLL FMSLRNACIH HHHHH.

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

    Interleukin 22 Human
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    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.

    More Info

    • 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
  • View Data Sheet

    Description:

    UL16 Binding Protein 3 Human Recombinant, Sf9

    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-2721

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    Description

    ULBP3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 430 amino acids (30-217a.a) and having a molecular mass of 49.3kDa.ULBP3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ULBP3 solution (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • 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

      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

      ADPDAHSLWY NFTIIHLPRH GQQWCEVQSQ VDQKNFLSYD CGSDKVLSMG HLEEQLYATD AWGKQLEMLR EVGQRLRLEL ADTELEDFTP SGPLTLQVRM SCECEADGYI RGSWQFSFDG RKFLLFDSNN RKWTVVHAGA RRMKEKWEKD SGLTTFFKMV SMRDCKSWLR DFLMHRKKRL EPTAPPTMAP GLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH

    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 Protein
  • View Data Sheet

    Description:

    Complement Factor Properdin Human Recombinant

    Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

    Product # :

    PRO-2011

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    Description

    CFP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (28-469 a.a.) and having a molecular mass of 50.9kDa.CFP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.

    • Synonyms

      Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

    • 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 MGSDPVLCFT QYEESSGKCK GLLGGGVSVE DCCLNTAFAY QKRSGGLCQP CRSPRWSLWS TWAPCSVTCS EGSQLRYRRC VGWNGQCSGK VAPGTLEWQL QACEDQQCCP EMGGWSGWGP WEPCSVTCSK GTRTRRRACN HPAPKCGGHC PGQAQESEAC DTQQVCPTHG AWATWGPWTP CSASCHGGPH EPKETRSRKC SAPEPSQKPP GKPCPGLAYE QRRCTGLPPC PVAGGWGPWG PVSPCPVTCG LGQTMEQRTC NHPVPQHGGP FCAGDATRTH ICNTAVPCPV DGEWDSWGEW SPCIRRNMKS ISCQEIPGQQ SRGRTCRGRK FDGHRCAGQQ QDIRHCYSIQ HCPLKGSWSE WSTWGLCMPP CGPNPTRARQ RLCTPLLPKY PPTVSMVEGQ GEKNVTFWGR PLPRCEELQG QKLVVEEKRP CLHVPACKDP EEEEL.

    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.

    Cfp Human
  • View Data Sheet

    Description:

    Interleukin-1 beta Mouse Recombinant

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    Product # :

    CYT-273

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    Description

    Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17500 Dalton. The IL-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Mouse IL-1b was lyophilized from a sterile filtered aqueous solution in 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.

    More Info

    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b 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-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.

    • Background

      What is the molecular weight/Mw of IL1B MOUSE Protein?
      IL1B MOUSE Protein has a total Mw of 17.5kDa.

      What is the source or expression system of IL1B MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL1B MOUSE Protein?
      IL1B MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1B MOUSE Protein?
      The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.

      What is the amino acid sequence of IL1B MOUSE Protein?
      MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.
      What applications can IL1B MOUSE Protein be used in?
      IL1B MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1B MOUSE Protein?
      The endotoxin level is minimal, IL1B 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.

    Il 1 Beta Mouse
  • View Data Sheet

    Description:

    Osteoprotegerin Human Recombinant, Hi-5

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

    Product # :

    CYT-633

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    Description

    Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Hi-5.

    Formulation

    Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.

    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.

    Osteoprotegerin Human Hi 5
  • View Data Sheet

    Description:

    Myostatin Human Recombinant, His Tag

    GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

    Product # :

    CYT-445

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    Description

    Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.

    • Synonyms

      GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add 0.1M Acetate buffer pH-4 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 10μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.

    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.

    Myostatin Human Fc
  • View Data Sheet

    Description:

    Activin-B Human Recombinant

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-058

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

    • Background

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

      What is the Purity of Activin B Protein?
      Activin B Protein is >97% pure as determined by SDS-PAGE.

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

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

    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.

    Activin B Human Plant
  • View Data Sheet

    Description:

    IL-6 Soluble Receptor Human Recombinant, Sf9

    IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2, Membrane glycoprotein 80, gp80, IL-6R, MGC104991.

    Product # :

    CYT-1077

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    • SDS-PAGE

    Description

    sIL6R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-365 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 355 amino acids and having a molecular mass of 39.6kDa.sIL6R purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    sIL6R protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit proliferation using M1 mouse myeloid leukemia cells. The ED50 range ≤ 20 ng/ml with Human IL-6.

    SDS-PAGE

    More Info

    • Introduction

      The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.

    • Synonyms

      IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2, Membrane glycoprotein 80, gp80, IL-6R, MGC104991.

    • 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

      ADPLAPRRCP AQEVARGVLT SLPGDSVTLT CPGVEPEDNA TVHWVLRKPA AGSHPSRWAG MGRRLLLRSV QLHDSGNYSC YRAGRPAGTV HLLVDVPPEE PQLSCFRKSP LSNVVCEWGP RSTPSLTTKA VLLVRKFQNS PAEDFQEPCQ YSQESQKFSC QLAVPEGDSS FYIVSMCVAS
      SVGSKFSKTQ TFQGCGILQP DPPANITVTA VARNPRWLSV TWQDPHSWNS SFYRLRFELR YRAERSKTFT TWMVKDLQHH CVIHDAWSGL RHVVQLRAQE EFGQGEWSEW SPEAMGTPWT ESRSPPAENE VSTPMQALTT NKDDDNILFR DSANATSLPV QDSSSVPLPH HHHHH

    • Background

      What is the molecular weight/Mw of SIL 6R HUMAN, SF9 Protein?
      SIL 6R HUMAN, SF9 Protein has a total Mw of 39.6kDa.

      What is the source or expression system of SIL 6R HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of SIL 6R HUMAN, SF9 Protein?
      SIL 6R HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of SIL 6R HUMAN, SF9 Protein?
      Measured by its ability to inhibit proliferation using M1 mouse myeloid leukemia cells. The ED50 range ≤ 20 ng/ml with Human IL-6.

      What is the amino acid sequence of SIL 6R HUMAN, SF9 Protein?
      ADPLAPRRCP AQEVARGVLT SLPGDSVTLT CPGVEPEDNA TVHWVLRKPA AGSHPSRWAG MGRRLLLRSV QLHDSGNYSC YRAGRPAGTV HLLVDVPPEE PQLSCFRKSP LSNVVCEWGP RSTPSLTTKA VLLVRKFQNS PAEDFQEPCQ YSQESQKFSC QLAVPEGDSS FYIVSMCVAS
      SVGSKFSKTQ TFQGCGILQP DPPANITVTA VARNPRWLSV TWQDPHSWNS SFYRLRFELR YRAERSKTFT TWMVKDLQHH CVIHDAWSGL RHVVQLRAQE EFGQGEWSEW SPEAMGTPWT ESRSPPAENE VSTPMQALTT NKDDDNILFR DSANATSLPV QDSSSVPLPH HHHHH.
      What applications can SIL 6R HUMAN, SF9 Protein be used in?
      SIL 6R HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for SIL 6R HUMAN, SF9 Protein?
      The endotoxin level is minimal, SIL 6R HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant SIL 6R HUMAN, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of SIL 6R HUMAN, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il6R Human
  • View Data Sheet

    Description:

    Coagulation Factor-IX, Mouse Antibody

    Product # :

    ANT-229

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

      Factor IX is a glycoprotein, which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 g-carboxyglutamic acid (gla) residues, which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180). Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A yields the intermediate IXa, which is subsequently converted to the fully active form IXab by cleavage at site B. The NH2-terminal light chain (GLA and EGF domains) remains covalently attached to the COOH-terminal heavy chain by a disulfide bond. The serine protease catalytic triad (Ser-365, His 221, Asp-269) is located in the heavy chain. Factor IXab is the catalytic component of the “intrinsic factor Xase complex” (factor VIIIa/IXa/Ca2+/phospholipid) which proteolytically activates factor X to factor Xa.

    • Solubility

      Reconstitute with H20 to get a 1 mg/ml concentration. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Human Factor-IX.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      NYRhFIX.

    • Applications

      Direct ELISA, Western Blot, imunohistochemistry. For W.B. use 1µg/ml of antibody.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4 C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20 C.

    • Purification Method

      Protein A.

    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.

    Factor Ix Antibody
  • View Data Sheet

    Description:

    Angiopoietin-like Protein 7 Human Recombinant

    angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein

    Product # :

    CYT-1208

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    Description

    ANGPTL7 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-346a.a) containing 553amino acids and having a molecular mass of 63.2kDa.ANGPTL7 is fused to a 233 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    ANGPTL7 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

      Angiopoietin-related protein 7 (ANGPTL7), belongs to the angiopoietin-like family of molecules. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera. ANGPTL7 production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-Beta and in cartilage by TNF-alpha.

    • Synonyms

      angiopoietin like 7, AngX, CDT6, dJ647M16.1, Angiopoietin-like factor; Angiopoietin-like Protein 7, ANGPTL7, angiopoietinrelated protein 7, Cornea-derived transcript 6 protein

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK

    • Background

      Angiopoietin-like Protein 7 Human Recombinant: An Emerging Player in Metabolic Regulation and Therapeutic Potential

      Abstract:

      Angiopoietin-like protein 7 (ANGPTL7) is a multifunctional protein that has recently gained attention for its potential role in metabolic regulation and as a therapeutic target for metabolic disorders. ANGPTL7 is involved in the modulation of lipid metabolism, adipogenesis, and insulin signaling. The availability of human recombinant ANGPTL7 protein has provided researchers with a valuable tool to unravel its biological functions and explore its therapeutic applications. This review provides an overview of the current knowledge on ANGPTL7 and discusses its potential as a therapeutic intervention in metabolic disorders.

      Introduction:

      Metabolic disorders, including obesity and type 2 diabetes, pose significant health challenges worldwide. ANGPTL7, a member of the angiopoietin-like protein family, has recently emerged as a potential regulator of metabolic processes. ANGPTL7 affects lipid metabolism, adipose tissue biology, and insulin signaling pathways, making it an intriguing target for therapeutic interventions in metabolic disorders.

      Role of ANGPTL7 in Metabolic Regulation:

      ANGPTL7 plays a multifaceted role in metabolic regulation. It influences lipid metabolism by regulating lipoprotein lipase (LPL) activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL7 also affects adipocyte biology and adipogenesis, potentially contributing to the development of obesity and related metabolic complications. Furthermore, ANGPTL7 modulates insulin signaling and glucose metabolism, suggesting its involvement in insulin resistance and diabetes pathogenesis.

      Mechanisms of ANGPTL7 Action:

      ANGPTL7 exerts its effects through various mechanisms. It interacts with extracellular matrix components, influencing cell adhesion and migration. ANGPTL7 also regulates angiogenesis and vascular remodeling, potentially linking it to metabolic regulation and tissue homeostasis.

      Therapeutic Potential of ANGPTL7 Human Recombinant Protein:

      The availability of ANGPTL7 human recombinant protein offers new avenues for therapeutic interventions in metabolic disorders. Modulating ANGPTL7 activity through recombinant protein administration or targeted interventions may have significant implications for lipid metabolism, adipose tissue function, and insulin sensitivity. Exploring ANGPTL7 as a therapeutic target holds promise for the development of novel strategies to tackle metabolic disorders.

      Conclusion:

      ANGPTL7 is an emerging player in metabolic regulation with potential therapeutic implications for metabolic disorders. Its involvement in lipid metabolism, adipose tissue biology, and insulin signaling pathways highlights its importance in maintaining metabolic homeostasis. The availability of ANGPTL7 human recombinant protein opens up new possibilities for further investigations and the development of targeted interventions for metabolic disorders.

      What is the molecular weight/Mw of ANGPTL7 Protein?
      ANGPTL7 Protein has a total Mw of 63.2kDa.

      What is the source or expression system of ANGPTL7 Protein?
      HEK293 cells.


      What is the Purity of ANGPTL7 Protein?
      ANGPTL7 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPTL7 Protein?
      The biological functionality of ANGPTL7 Protein will be determined in the future.

      What is the amino acid sequence of ANGPTL7 Protein?
      QKLSKHKTPA QPQLKAANCC EEVKELKAQV ANLSSLLSEL NKKQERDWVS VVMQVMELES NSKRMESRLT DAESKYSEMN NQIDIMQLQA AQTVTQTSAD AIYDCSSLYQ KNYRISGVYK LPPDDFLGSP ELEVFCDMET SGGGWTIIQR RKSGLVSFYR DWKQYKQGFG SIRGDFWLGN EHIHRLSRQP TRLRVEMEDW EGNLRYAEYS HFVLGNELNS YRLFLGNYTG NVGNDALQYH NNTAFSTKDK DNDNCLDKCA QLRKGGYWYN CCTDSNLNGV YYRLGEHNKH LDGITWYGWH GSTYSLKRVE MKIRPEDFKP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK

      What applications can ANGPTL7 Protein be used in?
      ANGPTL7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPTL7 Protein?
      The endotoxin level is minimal, ANGPTL7 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.

    Angptl7 Human
  • View Data Sheet

    Description:

    Growth Hormone Gilthead Seabream Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-529

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    Description

    Somatotropin Gilthead Seabream Recombinant Sparus Aurata produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.4 kDa. The Gilthead Seabream Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Binding assays of the 125I-labeled gilthead seabream GH to dolphin fish liver microsomal fraction resulted in high specific binding characterized by a Ka of 1.93 nM and a Bmax of 540 fmol/mg microsomal fraction protein. Recombinant gilthead seabream Growth Hormone, like ovine placental lactogen, exhibited growth-stimulating activity when applied orally to Sparus aurata larvae or intraperitoneally to juvenile fish.

    More Info

    • 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.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth-Hormone Gilthead Seabream although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Growth-Hormone Gilthead Seabream in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      AQPITDGQRLFSIAVSRVQHLHLLAQRLFSDFESSLQTEEQPQLNKIFLQ

      DFCNCDYIISPIDKHETQRSSVLKLLSISYRLVESWEFPSRSLSGGSAPR

      NQISPKLSELKTGIHLLIRANEDGAEIFPDRSALQLAPYGNYYQSLGTDE

      SLRRTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL

    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.

    Growth Hormone Seabream
  • View Data Sheet

    Description:

    Nucleotide Binding Protein 1 Human Recombinant

    Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 , NBP, NBP1, NBP35, Nucleotide-binding protein 1.

    Product # :

    PRO-2203

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    Description

    NUBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a) and having a molecular mass of 36.9kDa.NUBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques

    Source

    Escherichia Coli.

    Formulation

    NUBP1protein solution (1mg/ml) in Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 (NUBP1) is Involved in the regulation of centrosome duplication similarity. NUBP1 is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. NUBP1 is necessary for maturation of extra mitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer constructs a Fe-S scaffold complex, mediating the de novo compilation of a Fe-S cluster and its transfer to target apoproteins.

    • Synonyms

      Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 , NBP, NBP1, NBP35, Nucleotide-binding protein 1.

    • 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 MGSMEEVPHD CPGADSAQAG RGASCQGCPN QRLCASGAGA TPDTAIEEIK EKMKTVKHKI LVLSGKGGVG KSTFSAHLAH GLAEDENTQI ALLDIDICGP SIPKIMGLEG EQVHQSGSGW SPVYVEDNLG VMSVGFLLSS PDDAVIWRGP KKNGMIKQFL RDVDWGEVDY LIVDTPPGTS DEHLSVVRYL ATAHIDGAVI ITTPQEVSLQ DVRKEINFCR KVKLPIIGVV ENMSGFICPK CKKESQIFPP TTGGAELMCQ DLEVPLLGRV PLDPLIGKNC DKGQSFFIDA PDSPATLAYR SIIQRIQEFC NLHQSKEENL ISS.

    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.

    Nubp1 Human
  • View Data Sheet

    Description:

    Prothrombin Bovine

    Coagulation factor II, Prothrombin, F2.

    Product # :

    PRO-2759

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    Description

    Prothrombin bovine native.

    Source

    Bovine Plasma.

    Formulation

    The bovine prothrombin was lyophilized with no additives.

    More Info

    • Introduction

      Prothrombin produced in the liver is a vitamin K-dependent plasma protein. Before prothrombin is secreted into the plasma it goes through post translational modification by vitamin K-dependent carboxylase. The vitamin K-dependent carboxylase convertsprothrombin to 10 glutamic acid residues to gamma carboxyglutamic acid. Prothrombin comprises of 2 kringle regions which are found among residues a.a. 40 & 270 of the mature plasma protein and substitute the growth factor domains located in numerous plasma serine proteases.

    • Synonyms

      Coagulation factor II, Prothrombin, F2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bovine Prothrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Prothrombin should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles

    • Solubility

      It is recommended to reconstitute the lyophilized Bovine Prothrombin in sterile 0.9% NaCl

    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.

    Prothrombin Bovine
  • View Data Sheet

    Description:

    Interleukin-2 Mouse Recombinant

    Interleukin-2, T-cell growth factor (TCGF),  Lymphokine, IL-2.

    Product # :

    CYT-370

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    Description

    Interleukin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 17.2kDa. The IL-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution (1mg/ml) in 20mM PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

    More Info

    • Introduction

      IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

    • Synonyms

      Interleukin-2, T-cell growth factor (TCGF), Lymphokine, IL-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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 Mouse IL-2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

    • Background

      What is the molecular weight/Mw of IL 2 MOUSE Protein?
      IL 2 MOUSE Protein has a total Mw of 17.2kDa.

      What is the source or expression system of IL 2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL 2 MOUSE Protein?
      IL 2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 2 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

      What is the amino acid sequence of IL 2 MOUSE Protein?
      PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

      What applications can IL 2 MOUSE Protein be used in?
      IL 2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 2 MOUSE Protein?
      The endotoxin level is minimal, IL 2 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 2 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 2 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.482 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 calibrated solution of IL-2 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 2 Mouse
  • View Data Sheet

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by Gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • 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.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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.

    Leptin Human
  • View Data Sheet

    Description:

    Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-277

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    • SDS-PAGE

    Description

    NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      NAP 2 is supplied as a 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

      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

    • Background

      What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
      The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.

      What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

      What applications can CXCL7 95 A.A HUMAN Protein be used in?
      CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
      The endotoxin level is minimal, CXCL7 95 A.A HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL7 95 A.A HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL7 95 A.A HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.



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

    Nap 2 95 Aa Human
  • View Data Sheet

    Description:

    Macrophage Migration Inhibitory Factor, Mouse Anti Human

    Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.

    Product # :

    ANT-311

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    Formulation

    1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.

    • Immunogen

      Anti-human MIF mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human MIF amino acids 1-114 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P4E4AT.

    • Applications

      MIF antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      MIF antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Mif Antibody
  • View Data Sheet

    Description:

    Growth Hormone Human Recombinant, Plant

    GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-053

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    Description

    GH human Recombinant produced in Nicotiana benthamiana plant is a single chain containing 205 amino acids (molecular formula C1025H1570N280O306S7) and 6-His-tag at the N-terminal having the total molecular mass of 22.9kDa.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in PBS 0.05M buffer at pH 7.5.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The biological activity of human Growth Hormone is measured by cell proliferation using Nb2-11 cells. ED50 < 0.04-0.1 ng/mL.

    More Info

    • 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.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHFPTI PLSRPFDNAM LRAHRLHQLA FDTYQEFEEA YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE LLRISLLLIQ SWLEPVQFLR SVFANSLVYG ASDSNVYDLL KDLEEGIQTL MGRLEDGSPR TGQIFKQTYS KFDTNSHNDD ALLKNYGLLY CFRKDMDKVE TFLRIVQCRS VEGSCGFAG

    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.

    Gh Human Plant
  • View Data Sheet

    Description:

    Prolactin Receptor Antagonist, S. Active Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-1253

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    Description

    Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa was modified by additional 12 mutations. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

    Purity

    Greater than 97.0% as determined by:

    (a) Analysis by Gel Filtration.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis). It is ~ 100 fold more potent than 1-9 G129R hPRL in Ba/F3 cells and > 1000-fold potent in Nb2 cells.

    More Info

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr

    • Background

      Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

    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.

    Prlr Antagonist Human
  • View Data Sheet

    Description:

    Interleukin-7 Human Recombinant, HEK

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

    Product # :

    CYT-197

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    Description

    IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/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 IL-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 IL-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Background

      What is the molecular weight/Mw of IL7 HUMAN, HEK Protein?
      IL7 HUMAN, HEK Protein has a total Mw of 24.5kDa.

      What is the source or expression system of IL7 HUMAN, HEK Protein?
      HEK.
      What is the Purity of IL7 HUMAN, HEK Protein?
      IL7 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 HUMAN, HEK Protein?
      The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

      What applications can IL7 HUMAN, HEK Protein be used in?
      IL7 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 HUMAN, HEK Protein?
      The endotoxin level is minimal, IL7 HUMAN, HEK Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 HUMAN, HEK that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 HUMAN, HEK?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 7 Human Hek
  • View Data Sheet

    Description:

    Retinol Binding Protein-4 Mouse Recombinant, BioActive

    Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    Product # :

    CYT-1158

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    Description

    RBP4 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 191 amino acids (19-201 a.a) and having a molecular mass of 22.4kDa. RBP4 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The RBP4 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinol Binding Protein-4 or RBP4, is the retinol currier protein in the plasma. RBP4 takes part on the conversion of retinol to the stable and soluble retinol complex in the plasma. RBP4 carries retinol from the liver tissue where its store to peripheral tissues. RBP-retinol complex has interactions with transthyretin in the plasma, thus prevents its loss by filtration in the kidney.

    • Synonyms

      Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    • 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

      ERDCRVSSFR VKENFDKARF SGLWYAIAKK DPEGLFLQDN IIAEFSVDEK GHMSATAKGR VRLLSNWEVC ADMVGTFTDT EDPAKFKMKY WGVASFLQRG NDDHWIIDTD YDTFALQYSC RLQNLDGTCA DSYSFVFSRD PNGLSPETRR LVRQRQEELC LERQYRWIEH NGYCQSRPSR NSLLEHHHHH H.

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

    Rbp4 Mouse
  • View Data Sheet

    Description:

    Growth Hormone Mutant Zebrafish Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-709

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    Description

    Somatotropin Zebrafish Mutant G113R Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.18 kDa. The Zebrafish Mutant G113R Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3 pH-8.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • 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.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth-Hormone although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Zebrafish Mutant G113R in 0.4% NaHCO3 or water adjusted to pH-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Gln-Arg-Leu-Phe-Asn.

    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.

    Growth Hormone Zebrafish Mutant