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  • View Data Sheet

    Description:

    Interleukin-2 Receptor alpha Human Recombinant, sf9

    Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

    Product # :

    CYT-1020

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    Description

    IL2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (22-240 a.a.) and having a molecular mass of 52.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL2RA is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL2-Ra is one of the three constituent subunits of the IL2 receptor.
      IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.

    • Synonyms

      Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

    • 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

      ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

    • Background

      What is the molecular weight/Mw of CD25 HUMAN, SF9 Protein?
      CD25 HUMAN, SF9 Protein has a total Mw of 52.1kDa.

      What is the source or expression system of CD25 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CD25 HUMAN, SF9 Protein?
      CD25 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD25 HUMAN, SF9 Protein?
      The biological functionality of CD25 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CD25 HUMAN, SF9 Protein?
      ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

      What applications can CD25 HUMAN, SF9 Protein be used in?
      CD25 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD25 HUMAN, SF9 Protein?
      The endotoxin level is minimal, CD25 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CD25 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 CD25 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.

    Il2Ra Protein
  • View Data Sheet

    Description:

    Interleukin-36 Alpha 158 a.a. Human Recombinant

    Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

    Product # :

    CYT-179

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    Description

    IL36A 158 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 17.7kDa.The IL36A 158 a.a. Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated solution in 2xPBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    Fully biologically active when compared to standard. The specific activity determined by its ability in a functional ELISA. Immobilized rHuIL-36? at 1 ?g/mL can bind recombinant human IL-1 Rrp2 Fc Chimera with a range of 0.15-5?g/ml corresponding to a specific activity of 200,000-6,666,667IU/mg.

    More Info

    • Introduction

      Human IL-36a belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
      Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.

    • Synonyms

      Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36A 158 a.a. Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A 158 a.a. Human should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL36A 158 a.a. Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEKALKIDTP QQGSIQDINH RVWVLQDQTL IAVPRKDRMS PVTIALISCR HVETLEKDRG NPIYLGLNGL NLCLMCAKVG DQPTLQLKEK DIMDLYNQPE PVKSFLFYHS QSGRNSTFES VAFPGWFIAV SSEGGCPLIL TQELGKANTT DFGLTMLF

    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.

    Il36A 158 Aa Human
  • View Data Sheet

    Description:

    Interleukin-36 Beta 153 a.a Human Recombinant

    Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.

    Product # :

    CYT-180

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    Description

    IL36B 153 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (5-157a.a.) and having a molecular mass of 17.2kDa.The IL36B 153 a.a. Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as measured by its ability to induce IL-8 secretion in human preadipocytes is less than 10ng/ml, corresponding to a specific activity of 10IU/mg.

    More Info

    • Introduction

      Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner.

    • Synonyms

      Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36B 153 a.a. Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36B 153 a.a. Human should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL36B 153 a.a. Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      REAAPKSYAI RDSRQMVWVL SGNSLIAAPL SRSIKPVTLH LIACRDTEFS DKEKGNMVYL GIKGKDLCLF CAEIQGKPTL QLKEKNIMDL YVEKKAQKPF LFFHNKEGST SVFQSVSYPG WFIATSTTSG QPIFLTKERG ITNNTNFYLD SVE

    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.

    Il36B 153 Aa Human
  • View Data Sheet

    Description:

    Interleukin-22 Mouse Recombinant, Pegylated

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

    Product # :

    CYT-701

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    Description

    Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.

    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-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep

    • 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 White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 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.

    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 22 Mouse Pegylated
  • View Data Sheet

    Description:

    Interleukin-12 Mouse Recombinant

    NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-144

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    Description

    Interleukin-12 Mouse Recombinant produced in HEK 293 cells is a glycosylated disulfide linked heterodimeric polypeptide containing 506 amino acids and having a molecular weight of 75 kDa comprised of disulfide-bonded 35 kDa (p35) and 40 kDa (p40) subunits.The IL-12 is purified by proprietary chromatographic techniques.

    Source

    HEK-293 Cells.

    Formulation

    The protein was lyophilized from 0.5xPBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

    • Synonyms

      NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized mouse IL-12 although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution IL12 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 murine IL12 in sterile distilled pyrogen free water at 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.

      p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
      WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

    • Background

      What is the molecular weight/Mw of IL12 MOUSE Protein?
      IL12 MOUSE Protein has a total Mw of 75kDa.

      What is the source or expression system of IL12 MOUSE Protein?
      HEK-293 Cells.

      What is the Purity of IL12 MOUSE Protein?
      IL12 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 MOUSE Protein?
      IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

      What is the amino acid sequence of IL12 MOUSE Protein?
      p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.
      p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
      WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

      What applications can IL12 MOUSE Protein be used in?
      IL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 MOUSE Protein?
      The endotoxin level is minimal, IL12 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 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 IL12 MOUSE?
      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.

    Il12 Mouse
  • View Data Sheet

    Description:

    Interleukin-1 alpha Human Recombinant, His Tag

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    Product # :

    CYT-479

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    Description

    IL-1A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids fragment (113-271) with an amino-terminal hexahistidine tag and having a total molecular mass of 22.5kDa. The Interleukin-1 alpha His-tag is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-1 alpha His-tag protein is supplied in 1x PBS and 50% glycerol.

    Purity

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

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced by inflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    • 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. Please avoid freeze thaw cycles.

    • Background

      What is the molecular weight/Mw of IL1A HUMAN, HIS Protein?
      IL1A HUMAN, HIS Protein has a total Mw of 22.5kDa.

      What is the source or expression system of IL1A HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL1A HUMAN, HIS Protein?
      IL1A HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A HUMAN, HIS Protein?
      The biological functionality of IL1A HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL1A HUMAN, HIS Protein?
      IL1A HUMAN, HIS Protein is composed from 159 amino acids.

      What applications can IL1A HUMAN, HIS Protein be used in?
      IL1A HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1A HUMAN, HIS Protein?
      The endotoxin level is minimal, IL1A 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.

    Il 1 Alpha Human His
  • View Data Sheet

    Description:

    Interleukin-16 Human Recombinant, His Tag

    IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

    Product # :

    CYT-562

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    Description

    Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
      IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4.

    • Synonyms

      IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

    • Physical Appearance

      Sterile Filtered 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

      MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.

    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 16 Human His
  • View Data Sheet

    Description:

    Interleukin-24 Human Recombinant

    C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.

    Product # :

    CYT-515

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    Description

    Interleukin 24 human recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18 kDa. As a result of glycosylation, the protein migrates at 19.5 kDa on SDS-PAGE.

    Source

    Sacharomyces cerevisiae.

    Formulation

    Lyophilized from a 0.2µm filtered solution in PBS with BSA as a carrier.

    Purity

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

    Biological Activity

    Measured by its ability to bind to the cell receptor of Capan-1 cells line resulted in Stat-3 activation. The ED50 for this effect is typically 1.0 ng/ml, corresponding to a Specific Activity of 1x106 units/mg.

    More Info

    • Introduction

      IL24 is a member of the IL10 family of cytokines. It was identified as a gene induced during terminal differentiation in melanoma cells. IL-10B encoded can induce apoptosis selectively in various cancer cells. Overexpression IL-24 leads to elevated expression of several GADD family genes, which correlates with the induction of apoptosis. The phosphorylation of mitogen-activated protein kinase 14 (MAPK7/P38), and heat shock 27kDa protein 1 (HSPB2/HSP27) are found to be induced by this gene in melanoma cells, but not in normal immortal melanocytes. Alternatively spliced transcript variants encoding distinct isoforms have been reported. The glycosylation is essential for activity of IL-24. Functionally, IL-24 has diverse activities. At low concentrations, it induces type I proinflammatory cytokines such as IFN-g, IL-1b, IL-12 and TNF-a. At high concentration, it is a strong inducer of apoptosis in tumor cells, but not normal cells. mda-7/IL-24 is being hailed as a ‘magic bullet’ for cancer gene therapy.

    • Synonyms

      C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MDA7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MDA-7 Recombinant 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-24 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Il 24 Human
  • View Data Sheet

    Description:

    Interleukin-6 Human Recombinant

    B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    Product # :

    CYT-213

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    Description

    Interleukin-6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 21000 Dalton. The IL6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in 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 7TD1 cells is less than 0.1 ng/ml, corresponding to the specific activity of 1.0 x 10,000,000 Units per mg.

    More Info

    • Introduction

      Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

    • Synonyms

      B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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-6 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 Met-Pro-Val-Pro-Pro.

    • Background

      What is the molecular weight/Mw of IL 6 HUMAN Protein?
      IL 6 HUMAN Protein has a total Mw of 21kDa.

      What is the source or expression system of IL 6 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL 6 HUMAN Protein?
      IL 6 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 6 HUMAN Protein?
      The ED50 as determined by the dose-dependant stimulation of murine 7TD1 cells is less than 0.1 ng/ml, corresponding to the specific activity of 1.0 x 10,000,000 Units per mg.

      What is the amino acid sequence of IL 6 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Val-Pro-Pro.

      What applications can IL 6 HUMAN Protein be used in?
      IL 6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

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

      Who supplies recombinant IL 6 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 IL 6 HUMAN?
      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 0.47 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-6 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 6 Human
  • View Data Sheet

    Description:

    Interleukin-17E Mouse Recombinant

    IL-25, IL-17E, IL17E, IL25, Interleukin-25.

    Product # :

    CYT-641

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    Description

    Recombinant mouse IL-17E is a non-glycosylated, disulfide-linked homodimer, containing 2x145 amino acid chains, with a total molecular weight of 35.5 kDa. The Mouse IL-17E is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL17E was lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent production of IL-8 by human PBMCs and is 322-488ng/ml.

    More Info

    • Introduction

      IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
      IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.

    • Synonyms

      IL-25, IL-17E, IL17E, IL25, Interleukin-25.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Murine IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17E 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 IL17E in sterile 10mM HCl at a concentration not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VSLRIQEGCSHLPSCCPSKEQEPPEEWLKWSSASVS
      PPEPLSHTHHAESCRASKDGPLNSRAISPWSYELDRD
      LNRVPQDLYHARCLCPHCVSLQTGSHMDPLGNSVPL
      YHNQTVFYRRPCHGEEGTHRRYCLERRLYRVSLACV
      CVRPRVMA.

    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.

    Il17E Mouse
  • View Data Sheet

    Description:

    Interleukin-6 Mouse Recombinant, His Tag

    Interleukin-6, IL-6.

    Product # :

    CYT-845

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    • SDS-PAGE

    Description

    Interleukin-6 Mouse Recombinant produced in E.Coli migrates at 25kDa. Recombinant IL-6 Mouse is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    IL6 Mouse protein solution contains 25mM K2CO3 and PBS.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    SDS-PAGE

    More Info

    • Introduction

      Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.

    • Synonyms

      Interleukin-6, IL-6.

    • 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.

    • Background

      Research Paper on Interleukin-6 Mouse Recombinant, His Tag

      Abstract:

      Interleukin-6 (IL-6) Mouse Recombinant, tagged with His, is a cornerstone in unraveling the intricate web of immune modulation. This research paper delves into its molecular intricacies and its profound implications in immunological research. Through an exploration of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its pivotal role in shaping immune responses.

      Introduction:

      IL-6 Mouse Recombinant, bearing a His tag, has emerged as a pivotal tool in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.

      Molecular Features and His Tag Precision:

      Unveiling the molecular structure of IL-6 Mouse Recombinant, His Tag, we recognize its significance in facilitating purification and characterization. The His tag enhances our ability to study its functions with precision.

      Navigating Immune Responses:

      IL-6 plays a vital role in immune cell activation and inflammation. IL-6 Mouse Recombinant, His Tag, enables researchers to delve deeper into the cytokine's functions, shedding light on its impact on immune dynamics.

      Synonyms and Network Connections:

      Understanding the synonyms linked to IL-6, such as DIF, TNFA, and TNFSF2, enriches our comprehension of cytokine-mediated signaling networks. IL-6 Mouse Recombinant, His Tag, contributes to our understanding of these interconnected pathways.

      Potential Applications in Research and Therapy:

      Beyond laboratory research, IL-6 Mouse Recombinant, His Tag, holds therapeutic promise for immune-related disorders. Its utility in investigating disease mechanisms and evaluating therapeutic interventions marks it as a versatile tool.

      Clinical Implications and Future Avenues:

      The clinical relevance of IL-6 Mouse Recombinant, His Tag, is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its potential as a therapeutic intervention opens avenues for novel treatment strategies.

      Conclusion:

      In the intricate realm of immunology, IL-6 Mouse Recombinant, His Tag, stands as a valuable asset in understanding immune responses. Its molecular precision, pivotal functions, and potential therapeutic implications position it as an indispensable tool for advancing our knowledge of immune regulation.

      What is the molecular weight/Mw of IL6 MOUSE, HIS Protein?
      IL6 MOUSE, HIS Protein has a total Mw of 25kDa.

      What is the source or expression system of IL6 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL6 MOUSE, HIS Protein?
      IL6 MOUSE, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6 MOUSE, HIS Protein?
      The biological functionality of IL6 MOUSE, HIS Protein will be determined in the future.

      What applications can IL6 MOUSE, HIS Protein be used in?
      IL6 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL6 MOUSE, HIS Protein?
      The endotoxin level is minimal, IL6 MOUSE, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL6 MOUSE, HIS 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 IL6 MOUSE, HIS?
      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 6 His Mouse
  • View Data Sheet

    Description:

    TNF Ligand Superfamily Member 12 Human Recombinant

    TWEAK, TNF-related weak inducer of apoptosis, TNFSF12, DR3LG, Apo3-Ligand, APO3L, TNFRSF12A, Tumor necrosis factor ligand superfamily member 12, MGC20669, MGC129581.

    Product # :

    CYT-699

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    Description

    TNFSF12 Human Recombinant (94-249 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a total molecular mass of 18kDa. The TNFSF12 is fused with an 8 amino acids his tag at N-terminal (M-HHHHHH-R, total 164 a.a.) and purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in PBS.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using HUVECs, is less than 8ng/ml.

    More Info

    • Introduction

      TNFSF12 is a cytokine that is part of the TNF ligand family. TNFSF12 is a ligand for the FN14/TWEAKR receptor. TNFSF12 has overlapping signaling functions with TNF, but displays a much wider tissue distribution. TNFSF12 induces apoptosis through multiple pathways of cell death in a cell type-specific manner. TNFSF12 promotes proliferation and migration of endothelial cells, and therefore acts as a regulator of angiogenesis. TNFSF12 is expressed in adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK h induces NFkB and chemokine secretion. TNFSF12 exerts an apoptotic activity in HT-29 human adenocarcinoma cells whilst cultured in the presence of IFN-?. TNFSF12 promotes proliferation and migration of endothelial cells.

    • Synonyms

      TWEAK, TNF-related weak inducer of apoptosis, TNFSF12, DR3LG, Apo3-Ligand, APO3L, TNFRSF12A, Tumor necrosis factor ligand superfamily member 12, MGC20669, MGC129581.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TWEAK 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 TNFSF12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHRSA PKGRKTRARR AIAAHYEVHP RPGQDGAQAG VDGTVSGWEE ARINSSSPLR YNRQIGEFIV TRAGLYYLYC QVHFDEGKAV YLKLDLLVDG VLALRCLEEF SATAASSLGP QLRLCQVSGL LALRPGSSLR IRTLPWAHLK AAPFLTYFGL FQVH.

    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.

    Tnfsf12 Human
  • View Data Sheet

    Description:

    CD30 Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.

    Product # :

    CYT-824

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    Description

    TNFSF8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (63-234 a.a.) and having a molecular mass of 22kDa.TNFSF8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFSF8 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSD.

    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.

    Tnfsf8 Human
  • View Data Sheet

    Description:

    Parathyroid Hormone (1-84) N15 Labeled Human Recombinant

    Parathyrin, PTH, Parathormone.

    Product # :

    HOR-002

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    Description

    PTH (1-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 84 amino acids and having a molecular mass of 9550 Dalton labeled by the stable isotope N15.The PTH (1-84) N15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTH (1-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 9,000 Units/mg.

    More Info

    • Introduction

      Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
      In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
      In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
      Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures.

    • Synonyms

      Parathyrin, PTH, Parathormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.

    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.

    Pth 1 84 N15 Human
  • View Data Sheet

    Description:

    LIGHT Human Recombinant

    Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light

    Product # :

    CYT-1202

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    Description

    Recombinant Human LIGHT (74-240 aa) having a Mw of 23kDa was purified from E. coli.The Recombinant Human LIGHT is purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    TNFSF14 solution contains PBS & 25mM K2CO3.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light

    • 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

      DGPAGSWEQL IQERRSHEVN PAAHLTGANS SLTGSGGPLL WETQLGLAFL RGLSYHDGAL VVTKAGYYYI YSKVQLGGVG CPLGLASTIT HGLYKRTPRY PEELELLVSQ QSPCGRATSS SRVWWDSSFL GGVVHLEAGE KVVVRVLDER LVRLRDGTRS YFGAFMV

    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.

    Tnfsf14 Human
  • View Data Sheet

    Description:

    Mouse Anti Human Troponin I Type 1 Paired

    DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

    Product # :

    ANT-724

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    Description

    TNNI1 conjugation antibody and TNNI1 coating antibody are used to develop rapid test for TNNI1 rapid test.

    Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).

    Formulation

    * TNNI1 conjugation in 50mM Na-citrate, pH 6.0, 0.9% NaCl and 0.095 % NaN3.

    * TNNI1 coating antibody in 50mM Na-citrate, pH 6.0 0.9% NaCl and 0.095 % NaN3.

    Purity

    Greater than 95%.

    More Info

    • Introduction

      Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.

    • Synonyms

      DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

    • Physical Appearance

      2 vials of sterile Filtered clear colorless solution.

    • Applications

      Lateral flow immunoassay.

    • Type

      Mouse Anti Human Monoclonal.

    • Purification Method

      Purified monoclonal IgG by protein A 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.

    Tnni1 Paired Antibody
  • View Data Sheet

    Description:

    Cardiac Troponin-I Human

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2788

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    Description

    TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.

    Source

    Human heart tissue.

    Formulation

    TNNI3 was lyophilized from 0.01M HCl.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.

      While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.

      The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.

      The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.

      The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.

      By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.

    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.

    Cardiac Troponin 1 2
  • View Data Sheet

    Description:

    Progranulin Human Recombinant

    GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

    Product # :

    CYT-524

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    Description

    Progranulin Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 1-593 amino acids and having a molecular mass of 74kDa. The Progranulin is purified by standard chromatographic techniques.

    Source

    HEK 293 cells.

    Formulation

    The protein contains 1xPBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Activates phospho-ERK1/2 in neuronal mouse P19 cells and regulates food intake and body weight.

    More Info

    • Introduction

      A 88-kDa progranulin, also called proepithelin and PC cell-derived growth factor, is a single precursor protein of granulins which are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. Granulins are a variety of active, 6 kDa peptides and named granulin A (epithelin 1), granulin B (epithelin 2), granulin C, etc. Both the peptides and intact progranulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.

    • Synonyms

      GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Progranulin Human
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    Description:

    Cytomegalo Virus Pp65(UL83), 561 a.a.Recombinant

    Product # :

    CMV-218

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    Description

    The E.Coli derived 62.8 kDa recombinant protein contains the CMV Pp65 (UL83) immunodominant regions, having 561 amino acids.

    Source

    Escherichia Coli.

    Formulation

    25mM Tris-Hcl pH 8, 8M Urea, 5mM bMe.

    Purity

    CMV Pp65 protein is >95% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      CMV is part of the Betaherpesvirinae subfamily of Herpesviridae; including herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses has the common ability to stay latentover long periods of time. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

    • Stability

      CMV Pp65 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      CMV Pp65 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of CMV-infected individuals.

    • Purification Method

      CMV Pp65 was purified by proprietary chromatographic technique.

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

    Cmv Pp65 Ul83
  • View Data Sheet

    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

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    Description

    Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

    Purity

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

    More Info

    • Introduction

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant

      As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.

      Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.

      Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!

      How Does Bone Morphogenetic Protein-4 (BMP-4) Work?

      Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.

      The Role of BMP-4

      This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.

      However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:

      • Embryonic development
      • Wound healing
      • Bone remodeling
      • Immune response modulation
      • Tissue repair
      • Cardiac development and function

      What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?

      To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.

      As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.

      More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:

      • Cancer therapy
      • Development of engineered tissues and organs
      • Bone regeneration for the treatment of osteoporosis and nonunion fractures
      • Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
      • Promotion of tissue repair and regeneration

      Final Thoughts BMP-4

      Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.

      However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?
      The biological functionality of BMP4 Protein will be determined in the future.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human
  • View Data Sheet

    Description:

    Interleukin-8 (1-77 a.a.) Human Recombinant, (CXCL8) Pichia

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-349

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    Description

    Interleukin-8 Human Recombinant produced in Yeast is a single, glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9 kDa. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium phosphate buffer pH-8.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Chemotactic activity was reached at 25ng/ml on human neutrophils.

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.
      When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN, PICHIA Protein?
      CXCL8 HUMAN, PICHIA Protein has a total Mw of 9kDa.

      What is the source or expression system of CXCL8 HUMAN, PICHIA Protein?
      Pichia Pastoris.

      What is the Purity of CXCL8 HUMAN, PICHIA Protein?
      CXCL8 HUMAN, PICHIA Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, PICHIA Protein?
      Chemotactic activity was reached at 25ng/ml on human neutrophils.

      What is the amino acid sequence of CXCL8 HUMAN, PICHIA Protein?
      CXCL8 HUMAN, PICHIA Protein is composed from 79 amino acids.

      What applications can CXCL8 HUMAN, PICHIA Protein be used in?
      CXCL8 HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN, PICHIA Protein?
      The endotoxin level is minimal, CXCL8 HUMAN, PICHIA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 HUMAN, PICHIA 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 CXCL8 HUMAN, PICHIA?
      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 8 77 Human Pichia
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    Description:

    Thyroglobulin Human, Biotinylated

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2563

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    Description

    Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).

    Source

    Native, Isolated from human thyroid glands.

    Formulation

    Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
      Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Thyroglobulin Protein
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    Description:

    Cystatin-C Mouse Recombinant, Active

    Cystatin-C, Cystatin-3,  Cst3,  CST3    

    Product # :

    PRO-2433

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    Description

    CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Cst3, CST3

    • 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

      ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA 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.

    Cst3 Mouse Active
  • View Data Sheet

    Description:

    Interleukin-1 Alpha Porcine Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    Product # :

    CYT-396

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    Description

    Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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-1 alpha 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 Ser-Ala-Thr-Tyr-Ser.

    • Background

      What is the molecular weight/Mw of IL1A PORCINE Protein?
      IL1A PORCINE Protein has a total Mw of 18kDa.

      What is the source or expression system of IL1A PORCINE Protein?
      Escherichia Coli.

      What is the Purity of IL1A PORCINE Protein?
      IL1A PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A PORCINE Protein?
      The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

      What is the amino acid sequence of IL1A PORCINE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.

      What applications can IL1A PORCINE Protein be used in?
      IL1A PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1A PORCINE Protein?
      The endotoxin level is minimal, IL1A PORCINE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 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-1 as a Reference Standard.

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    Il 1 Alpha Porcine