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  • MEC (CCL28)

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    Eotaxin (CCL11,24,26)

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  • Actin

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  • Aprotinin

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Search results

1000 results found for “prothymosin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    Buserelin

    Description:

    Buserelin

    Product # :

    HOR-255

    Price :

    Quantity :

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    Description

    Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.

    Formulation

    The Buserelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Buserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Buserelin 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 Buserelin in sterile 18MΩ-cm H2O not less than 100 µg/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.

    Buserelin
  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) YopB

    Description:

    Yersinia Enterocolitica (O:9) YopB Recombinant

    Protein YopD, pYV0054.

    Product # :

    PRO-2575

    Price :

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    • More Info

    Description

    Recombinant Yersinia Enterocolitica (O:9) YopB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain having a calculated molecular mass of 43kDa. Y.Enterocolitica (O:9) YopB is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Y.Enterocolitica (O:9) YopB is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gastroenteritis which has been identified as caused by Yersinia Enterocolitica has been discovered by virulent isolates of the bacteria. During infection, pores are being formed in the presence of adapter protein Yersiniosis. YopB's Interaction with the target membrane to form pores enables the entrance of YopE effectors to the cytoplasmic space of the host’s cell.

    • Synonyms

      Protein YopD, pYV0054.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Activity

      1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with 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.

    Yopb Protein
  • View Data Sheet

    Name :

    IL19 Human, HEK

    Description:

    Interleukin-19 Human Recombinant, HEK

    Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19

    Product # :

    CYT-1192

    Price :

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    Description

    IL19 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-177) containing 164 amino acids and having a molecular mass of 19.1 kDa.IL19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    IL19 protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. IL19 binds the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.

    • Synonyms

      Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19

    • 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

      DGSHMLRRCL ISTDMHHIEE SFQEIKRAIQ AKDTFPNVTI LSTLETLQII KPLDVCCVTK NLLAFYVDRV FKDHQEPNPK ILRKISSIAN SFLYMQKTLR QCQEQRQCHC RQEATNATRV IHDNYDQLEV HAAAIKSLGE LDVFLAWINK NHEVMFSAHH HHHH

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

    Il19 Human
  • View Data Sheet

    Name :

    IL1A Human, HEK

    Description:

    Interleukin-1 alpha Human Recombinant, HEK

    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-964

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • biological activity
    • More Info

    Description

    Interleukin-1 alpha Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 18kDa due to glycosylation.The IL1A is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL-1A protein was lyophilized from a 0.2µm filtered solution of PBS pH 7.4 with 10% trehalose as protectant.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x109 unit/mg.

    More Info

    • Introduction

      IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.

    • 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 IL-1A 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 IL1A in deionized water to a stock solution of 0.5mg/ml.

    • Background

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

      What is the source or expression system of IL1A HUMAN, HEK Protein?
      HEK.
      What is the Purity of IL1A HUMAN, HEK Protein?
      IL1A HUMAN, HEK Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A HUMAN, HEK Protein?
      Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x109 unit/mg.

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

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

    Il1A Human Hek
  • View Data Sheet

    Name :

    Lamin-A Human

    Description:

    Lamin-A Human Recombinant

    Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    Product # :

    PRO-690

    Price :

    Quantity :

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    More Info

    • description
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    • More Info

    Description

    Recombinant Human Lamin A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids and having a molecular mass of 70 kDa. Lamin-A protein is fused to a 6xHis tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Lamin-A Protein solution (0.9mg/ml) contains 20mM phosphate buffer pH 7.0, 500mM NaCl, 1mM DTT, 1.5mM EDTA and 20% (v/v) Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
      Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
      Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

    • Synonyms

      Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    • 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. Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
      EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
      RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
      QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
      LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
      RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
      TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
      KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
      WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
      RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRS

    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.

    Lamin A
  • View Data Sheet

    Name :

    ACTH

    Description:

    Adrenocorticotropic Hormone

    Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    Product # :

    HOR-279

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    Description

    The Molecular formula of Adrenocorticotropic Hormone is C136H210N40O31S and the molecular weight is 2933.5 Dalton.

    Formulation

    The ACTH hormone was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Adrenocorticotropic hormone, as its name implies, stimulates the adrenal cortex. More specifically, it stimulates secretion of glucocorticoids such as cortisol, and has little control over secretion of aldosterone, the other major steroid hormone from the adrenal cortex. Stimulates secretion of adrenal corticosteroids and induces growth of adrenal cortex. ACTH also called Tetracosactide directly activates G-proteins. A stimulator of adenylate cyclase and cAMP formation.

    • Synonyms

      Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-OH.

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

    Acth
  • View Data Sheet

    Name :

    HNMT Human, Active

    Description:

    Histamine N-Methyltransferase Human Recombinant, Active

     HMT, HNMT-S1, HNMT-S2, MRT51.

    Product # :

    ENZ-1071

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    Description

    HNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-292 a.a) and having a molecular mass of 37.4kDa. HNMT is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HNMT protein solution (1mg/ml) containing 20mM, Tris-Hcl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 200 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37°C.

    More Info

    • Introduction

      Histamine N-Methyltransferase or HNMT, is located in the cell cytosol. Sadenosyl-L-methionine acts as a methyl donor for HNMT which inactivates histamine. By inactivation of histamine, it affects the immune system’s response. HNMT acts on histamine in body tissues such as kidney, central nervous system and bronchus. The protein has a crucial part in the airway response to histamine & histamine degradation process and regulation.

    • Synonyms

      HMT, HNMT-S1, HNMT-S2, MRT51.

    • Physical Appearance

      Sterile Filtered clear 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).Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS MRSLFSDHGK YVESFRRFLN HSTEHQCMQE FMDKKLPGII GRIGDTKSEI KILSIGGGAG EIDLQILSKV QAQYPGVCIN NEVVEPSAEQ IAKYKELVAK TSNLENVKFA WHKETSSEYQ SRMLEKKELQ KWDFIHMIQM LYYVKDIPAT LKFFHSLLGT NAKMLIIVVS GSSGWDKLWK KYGSRFPQDD LCQYITSDDL TQMLDNLGLK YECYDLLSTM DISDCFIDGD ENGDLLWDFL TETCNFNATA PPDLRAELGK DLQEPEFSAK KEGKVLFNNT LSFIVIEA.

    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.

    Hnmt Protein
  • View Data Sheet

    Name :

    TNF a Mutant Human

    Description:

    Tumor Necrosis Factor-Alpha Mutant Human Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-384

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    Description

    Tumor Necrosis Factor-a Variant Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 151 amino acids and having a molecular mass of 16598 Dalton. The TNF-alpha Variant is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized after extensive dialysis against 0.5x PBS pH -7.

    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 cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 units/mg.

    More Info

    • Introduction

      The clinical use of the potent anti-tumor activity of TNF-a has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-a mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-a, which binds to the murine TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-a, which binds to both murine TNF receptors. Based on these results, many TNF-? mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.
      Recombinant Human TNF-a Variant/Mutant compared with the wild-type, has an amino acid sequence deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven tohave more activity and with less inflammatory side effect in vivo.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN
      QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIAF.

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

    Tnf Alpha Mutant Human
  • View Data Sheet

    Name :

    Flt3 Ligand Human, HEK

    Description:

    Flt3-Ligand Human Recombinant, HEK derived

    Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    Product # :

    CYT-706

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    Description

    Flt3-Ligand Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 24-30kDa due to glycosylation. The Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Flt3-Ligand was lyophilized from a 0.2µm filtered solution containing 1xPBS.

    Purity

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

    Biological Activity

    The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.

    More Info

    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND HUMAN, HEK Protein?
      FLT3 LIGAND HUMAN, HEK Protein has a total Mw of 27kDa.

      What is the source or expression system of FLT3 LIGAND HUMAN, HEK Protein?
      HEK293 (Human Embryonic Kidney cell line).

      What is the Purity of FLT3 LIGAND HUMAN, HEK Protein?
      FLT3 LIGAND HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND HUMAN, HEK Protein?
      The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.

      What is the amino acid sequence of FLT3 LIGAND HUMAN, HEK Protein?
      TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.

      What applications can FLT3 LIGAND HUMAN, HEK Protein be used in?
      FLT3 LIGAND HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND HUMAN, HEK Protein?
      The endotoxin level is minimal, FLT3 LIGAND HUMAN, HEK 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.

    Flt3 Ligand Human Hek
  • View Data Sheet

    Name :

    S.Typhi H

    Description:

    Salmonella Typhi H Antigen Recombinant

    Product # :

    STY-001

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    Description

    Recombinant Salmonella Typhi H Antigen produced in E.coli is full length flagellin sequence and fused to a 6 His Tag at C-terminus, migrating as a 35kDa band on SDS-PAGE.S. typhi H antigen is a flagellin protein, which strongly reacts to specific IgM and IgG produced in infected patients.

    Source

    Escherichia Coli.

    Formulation

    Sterile Filtered solution containing PBS and 25mM arginine.

    Purity

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

    More Info

    • Introduction

      Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      S.Typhi H although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay.

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    Styphi H
  • View Data Sheet

    Name :

    Protein-A/G Cys

    Description:

    Protein A/G Cys Recombinant

    Product # :

    PRO-1928

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    • sds-page, HPLC

    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by HPLC.
    (b) Analysis by SDS-PAGE.

    sds-page, HPLC

    protein a/g cys hplc - Product image 1
    protein a/g cys sds-page - Product image 2

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEC.

    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.

    Protein A G Cys
  • View Data Sheet

    Name :

    Treponema p17 16.4kDa

    Description:

    Treponema pallidum p17, 16.4kDa Recombinant

    Product # :

    TRP-252

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    Description

    Recombinant Treponema p17 produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 16.4kDa and fused to a His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Treponema p17 although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Treponema p17 in sterile 18M-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.

    Treponema P17 164Kda
  • View Data Sheet

    Name :

    RPS27A Human, Biotin

    Description:

    Ubiquitin Biotinylated Human Recombinant

    Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

    Product # :

    PRO-629

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    Description

    Recombinant Human RPS27A protein biotinylated with NHS-biotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 76 amino acids and having a molecular mass of 8.6 kDa.

    Source

    Escherichia Coli.

    Formulation

    The RPS27A is supplied in 1x PBS and 0.05% PBS.

    Purity

    RPS27A Protein biotinilation is determined by Western Blotting and ELISA analysis using streptavidin–HRP conjugated as a detection reagent. Free biotin is eliminated by dialysis against PBS. Protein concentration is determined by 280nm absorbance.

    More Info

    • Introduction

      Recombinant Human Ubiquitin having the accession number of P62988 was conjugated to Biotin. RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
      RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
      The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein.

    • Synonyms

      Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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 prevent freeze-thaw cycles.

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

    RPS27A Human, Biotin
  • View Data Sheet

    Name :

    Bremelanotide

    Description:

    Bremelanotide

    PT-141, Rekynda, bremelanotide acetate.

    Product # :

    HOR-039

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    Description

    Bremelanotide Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 1025.16 Dalton and a Molecular formula of C50H68N40O10.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Synonyms

      PT-141, Rekynda, bremelanotide acetate.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ac-Nle-cyclo(-Asp-His-D-Phe-Arg-Trp-Lys)-OH.

    • Background

      Bremelanotide (PT-141), a synthetic heptapeptide, is a novel therapeutic agent primarily utilized for the treatment of sexual dysfunction. This paper provides an exhaustive review of Bremelanotide, detailing its biochemical structure, mechanism of action, therapeutic applications, and future prospects in clinical medicine.

      Bremelanotide (PT-141), derived from Melanotan II, is a synthetic peptide developed for its role in treating sexual dysfunction in both men and women (Clayton et al., 2016). This paper presents a comprehensive examination of Bremelanotide, its biological properties, and potential therapeutic uses.

      Bremelanotide acts as a non-selective agonist of the melanocortin receptors, primarily MC3R and MC4R, present in the central nervous system. The peptide initiates its action in the hypothalamus, leading to downstream effects on sexual desire and arousal (King et al., 2007).

      The US Food and Drug Administration approved Bremelanotide for the treatment of premenopausal women with hypoactive sexual desire disorder (HSDD) in 2019. In clinical trials, it demonstrated efficacy in enhancing sexual desire and reducing distress associated with HSDD (Kingsberg et al., 2019).

      While the current focus of Bremelanotide is on treating sexual dysfunction, its future potential may extend to other areas due to its unique mechanism of action. Further research is needed to explore the full therapeutic potential of this intriguing peptide. In conclusion, Bremelanotide represents a significant advance in sexual dysfunction therapeutics, with potential implications extending beyond this realm.

    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.

    Bremelanotide
  • View Data Sheet

    Name :

    GAL Human

    Description:

    Galanin Prepropeptide Human Recombinant

    GALN, GLNN, GMAP, GAL, GAL1.

    Product # :

    PRO-1433

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    • More Info

    Description

    GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.

    • Synonyms

      GALN, GLNN, GMAP, GAL, GAL1.

    • 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 MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.

    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.

    Gal Human
  • View Data Sheet

    Name :

    Collagen-I Goat

    Description:

    Goat Collagen-I

    Product # :

    PRO-2682

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    Description

    Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Goat tissues.

    Formulation

    Collagen-I was lyophilized without additives.

    Purity

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

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-I although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-I 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 Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution 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.

    Collagen I Goat
  • View Data Sheet

    Name :

    MIF Human His N

    Description:

    Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus

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

    Product # :

    CYT-431

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    Description

    MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing PBS pH-7.4.

    Purity

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

    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.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

    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 Human His N
  • View Data Sheet

    Name :

    HTLV-1 mosaic

    Description:

    HTLV-1 Mosaic Recombinant

    Product # :

    HIV-144

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    Description

    The E.Coli derived recombinant mosiac protein contains the gp21 and gp46 immunodominant regions, 374-400 amino acids and 190-201 amino acids. The protein is fused with GST at N-terminus.

    Formulation

    20mM Phosphate buffer PH 7.5.

    Purity

    Protein is >95% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      Human T-lymphotropic virus (HTLV) is a human, single-stranded RNA retrovirus that causes T-cell leukemia and T-cell lymphoma. The virus activates a subset of T-helper cellscalled Th1cells. The result is a proliferation of Th1 cells and overproduction of Th1 related cytokines (mainly IFN-gamma and TNF-alpha). Feedback mechanisms of these cytokines cause a suppression of the Th2 lymphocytes and a reduction of Th2 cytokine production (mainly IL-4, IL-5, IL-10 and IL-13). The end result is a reduction in the ability of the infected host to mount an adequate immune response to invading organisms that require a predominantly Th2 dependant response (these include parasitic infections and production of mucosal and humoral antibodies).

    • Stability

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

    • Applications

      HTLV-1 Mosaic can be used as an antigen in ELISA and Western Blots. Excellent reagent for correct detection of HTLV infections, with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HTLV-I infected individuals

    • Purification Method

      HTLV-1 Mosaic 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.

    Htlv 1 Mosaic
  • View Data Sheet

    Name :

    TH Mouse

    Description:

    Tyrosine Hydroxylase Mouse Recombinant

    Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    Product # :

    ENZ-988

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    Description

    TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TH protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.

    • Synonyms

      Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    • 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

      ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.

    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.

    Th Mouse
  • View Data Sheet

    Name :

    HSPB8 Human, His

    Description:

    Heat Shock 22kDa Protein 8 Human Recombinant, His Tag

    HSPB8, H11, HMN2, CMT2L, DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein beta-8, Alpha-crystallin C chain, Small stress protein-like protein HSP22, E2-induced gene 1 protein, Protein kinase H11, CRYAC.

    Product # :

    HSP-031

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    Description

    HSPB8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 23.7kDa. The HSPB8 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The HSPB8 protein solution contains 20mM Tris-HCl pH-8, 100mM NaCl, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSPB8 is part of the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. HSPB8 is induced by estrogen in estrogen receptor-positive breast cancer cells. HSPB8 protein functions as a chaperone in association with BAG3, a stimulator of macroautophagy. HSPB8 participates in the regulation of cell proliferation, apoptosis, and carcinogenesis. Mutations in HSPB8 gene have been related with different neuromuscular diseases, including Charcot-Marie-Tooth disease.

    • Synonyms

      HSPB8, H11, HMN2, CMT2L, DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein beta-8, Alpha-crystallin C chain, Small stress protein-like protein HSP22, E2-induced gene 1 protein, Protein kinase H11, CRYAC.

    • 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 MADGQMPFSC HYPSRLRRDP FRDSPLSSRL LDDGFGMDPF PDDLTASWPD WALPRLSSAW PGTLRSGMVP RGPTATARFG VPAEGRTPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PVTVFASLSP EGLLIIEAPQ VPPYSTFGES SFNNELPQDS QEVTCT.

    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.

    Hspb8 Human His
  • View Data Sheet

    Name :

    SLC51B Human

    Description:

    Solute Carrier Family 51 Beta Human Recombinant

    OSTB, OSTBETA, Organic solute transporter subunit beta, OST-beta, Solute carrier family 51 subunit beta.

    Product # :

    PRO-1727

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    Description

    SLC51B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (57-128 a.a) and having a molecular mass of 10.7kDa.SLC51B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SLC51B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Solute Carrier Family 51 Beta (SLC51B), is a protein coding gene. SLC51B is an organic solute transporter subunit. SLC51 is composed of twodifferent proteins that must heterodimerize to generate transport activity, however the role of the individual subunits inmediating transport activity is unknown. The results show that SLC51B is required for both proper traffickingof SLC51A and formation of the functional transport unit, and identify specific residues of SLC51B essential for theseprocesses. Among the diseases associated with SLC51B are extrahepatic cholestasis, and biliary atresia.

    • Synonyms

      OSTB, OSTBETA, Organic solute transporter subunit beta, OST-beta, Solute carrier family 51 subunit beta.

    • 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 MGSRSIQASR KEKMQPPEKE TPEVLHLDEA KDHNSLNNLR ETLLSEKPNL AQVELELKER DVLSVFLPDV PETES

    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.

    Slc51B Human
  • View Data Sheet

    Name :

    IL 2 Human, His

    Description:

    Interleukin-2 Human Recombinant, His Tag

    T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

    Product # :

    CYT-666

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    Description

    Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 133 amino acids fragment (21-153) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-2 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-2 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    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

      T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

    • 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.

    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 2 Human His
  • View Data Sheet

    Name :

    Epoetin Human, Sf9

    Description:

    Erythropoietin-alpha Human Recombinant, Sf9

    Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

    Product # :

    CYT-934

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    • sds-page

    Description

    Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPO-a is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EPO a protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.

    sds-page

    Epoetin-sds-page - Product image 1

    More Info

    • Introduction

      This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      Erythropoietin, Epoetin, MVCD2, EP, Erythropoietin-Alpha, EPO-a, EPO-alpha.

    • 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

      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 19.5kDa.

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

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

      What is the Biological Activity of EPOETIN Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is ≤ 0.5 ng/ml.

      What is the amino acid sequence of EPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

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

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

    Epo A Human Sf9
  • View Data Sheet

    Name :

    CCM2 Human

    Description:

    Cerebral Cavernous Malformation 2 Human Recombinant

    Cerebral Cavernous Malformation 2, C7orf22, malcavernin, Cerebral Cavernous Malformations 2 Protein, Chromosome 7 Open Reading Frame 22, OSM, MGC4067.

    Product # :

    PRO-1825

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    Description

    CCM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (66-353 a.a) and having a molecular mass of 34.3kDa.CCM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCM2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cerebral Cavernous Malformation 2, also known as CCM2 is a piece of the CCM signaling pathway which is a vital regulator of heart and vessel formation as well as integrity. CCM2 performs through the stabilization of endothelial cell junctions. In addition, CCM2 functions as a scaffold protein for MAP2K3-MAP3K3 signaling. CCM2 plays a key role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock. Mutations in CCM2 result in cerebral cavernous malformations. Multiple transcript variants encoding dissimilar isoforms have been discovered for CCM2.

    • Synonyms

      Cerebral Cavernous Malformation 2, C7orf22, malcavernin, Cerebral Cavernous Malformations 2 Protein, Chromosome 7 Open Reading Frame 22, OSM, MGC4067.

    • 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 MGSEVKYLGQ LTSIPGYLNP SSRTEILHFI DNAKRAHQLP GHLTQEHDAV LSLSAYNVKL AWRDGEDIIL RVPIHDIAAV SYVRDDAAHL VVLKTDDSST KVDIKETYEV EASTFCFPES VDVGGASPHS KTISESELSA SATELLQDYM LTLRTKLSSQ EIQQFAALLH EYRNGASIHE FCINLRQLYG DSRKFLLLGL RPFIPEKDSQ HFENFLETIG VKDGRGIITD SFGRHRRALS TTSSSTTNGN RATGSSDDRS APSEGDEWDR MISDISSDIE ALGCSMDQDS 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.

    Ccm2 Human
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