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1000 results found for “Lipocalin”
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Name :
Insulin Human, HisDescription:
Insulin Human Recombinant, His Tag
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Product # :
CYT-1076Price :
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Shipped with Ice Packs
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Description
Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Insulin protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MCF7 human breast cancer cell. The ED50 for this effect is less or equal to 4 ug/ml.
More Info
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Introduction
Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFVNQHLC GSHLVEALYL VCGERGFFYT PKTRREAEDL QVGQVELGGG PGAGSLQPLA LEGSLQKRGI VEQCCTSICS LYQLENYCN
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LA/SS-B Human, BiotinDescription:
LA / SS-B Human Recombinant, Biotinylated
Lupus La protein, Sjoegren syndrome type B antigen, SS-B, La ribonucleoprotein, La autoantigen, SSB, La, LARP3, LA/SS-B, La(SS-B).
Product # :
PRO-2562Price :
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Description
LA/SS-B Human Recombinant produced in SF9 is a single, glycosylated, polypeptide chain having a calculated molecular mass of 48 kDa. The LA/SS-B is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
The protein solution contains 20mM HEPES, pH 7.5, 400mM NaCl, 20% Glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
The La protein is a 47 kDa polypeptide that frequently acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients. La is involved in various aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III - transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs linked to hepatitis C virus. It occurs in both the nucleus and the cytoplasm, where it assumes different roles. In the nucleus, La protein facilitates the production of tRNAs, acting as an RNA polymerase III (RNAP III) transcription factor by attaching to the U-rich 3'UTR of nascent transcripts, aiding in their folding and maturation. In the cytoplasm, La protein facilitates the translation of specific mRNAs, acting as a translation factor. As an RNA binding protein (RBP), La protein associates with subsets of mRNAs which contain a 5'-terminal oligopyrimidine (5'TOP) motif known to direct protein synthesis. The binding of La protein to particular classes of RNA molecules regulates their downstream processing, guards them from endonuclease digestion, and organizes their export from the nucleus. La/SS-B appears to be readily disposed to proteolysis, which results in many smaller (42kD, 320, and 270) nevertheless still immunoreactive polypeptides. La/SS-B antigen is strongly conserved across species. Anti-La/SS-B autoantibodies were originally found as precipitating autoantibodies in sera of Sjogren's Syndrome patients and referred to as SjT. Anti-La/SS-B precipitins are most frequently found in Sjogren's Syndrome, Systemic Lupus Erythematosus (SLE) and Subacute Cutaneous Lupus. Also, there seems to be a correlation between anti-La/SS-B and the absence of nephritis in SLE patients.
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Synonyms
Lupus La protein, Sjoegren syndrome type B antigen, SS-B, La ribonucleoprotein, La autoantigen, SSB, La, LARP3, LA/SS-B, La(SS-B).
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. 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.
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Name :
OPG HumanDescription:
Osteoprotegerin Human Recombinant
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-177Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant Human Osteoprotegerin produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of 20kDa. The OPG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OPG was lyophilized from a 0.2µm filtered concentrated (0.5mg/ml) solution in PBS, pH 7.4.
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 its ability to neutralize the stimulation of U937 cells treated with 10ng/ml of soluble RANKL corresponding to a specific activity of 100,000IU/mg.More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
METFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL-12 HumanDescription:
Interleukin-12 Human Recombinant
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Product # :
CYT-101Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-12 Human Recombinant produced in HEK cells is a glycosylated heterodimer, having a total molecular weight of 57kDa.The IL12 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
IL12 was lyophilized from a 0.2µm filtered solution containing 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
The EC50 is 0.5ng/ml.More Info
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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. IL-12 is an initiator of cell-mediated immunity.
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Synonyms
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-12 although stable at room temperature for 3 weeks, should be stored desiccated 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.
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Solubility
It is recommended to reconstitute the lyophilized IL12 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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Amino Acid Sequence
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
>IL-12 A
RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
>IL-12B
IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 12 p40 Human BaculovirusDescription:
Interleukin-12 p40 Human Recombinant, Baculovirus
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
Product # :
CYT-134Price :
Quantity :
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Shipped with Ice Packs
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Description
IL 12 p40 Human Recombinant produced in Hi-5 cell using Baculovirus is a single polypeptide chain containing 315 amino acids (23-328) and having a molecular mass of 35.8kDa.IL 12 p40 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Baculovirus
Formulation
The IL 12 p40 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 100mM PMSF and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH HHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 23 Human, HisDescription:
Interleukin-23 Human Recombinant, His Tag
Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.
Product # :
CYT-067Price :
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Description
Recombinant Human Interleukin-23 produced in Sf9 Baculovirus cells is a glycosylated heterodimer composed of 2 disulfide-linked subunits. A p19 subunit which is unique to IL23 and a p40 subunit which is shared with IL12. The p19 subunit/IL23A (20-189aa, total of 176 aa, MW 19.5kDa) and p40 subunit /IL12B (23-328aa, total of 306 aa, MW 34.6kDa), the total predicted molecular mass of 54.1kDa (Molecular weight on SDS-PAGE will appear higher). IL23 is fused to a 6 aa His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL23 protein solution (1mg/ml) contains PBS (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
IL23 is composed of a subunit of the heterodimeric cytokine IL23 and the p40 subunit of interleukin 12 (IL12B). Interleukin-23 (IL-23) belongs to the IL-12 family and is produced by antigen presenting cells. IL-23 using IL12RB1 and IL-23R (specific for IL-23) can activate STAT and NF-kB pathways and stimulate the production of interferon-gamma. ). IL-23 is known to take a vital part in the inflammation process and is associated with auto immune diseases. However, unlike IL12, which acts primarily on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells.
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Synonyms
Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
IL12B: IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.
IL23A: RAVPGGSSPA WTQCQQLSQK LCTLAWSAHP LVGHMDLREE GDEETTNDVP HIQCGDGCDP QGLRDNSQFC LQRIHQGLIF YEKLLGSDIF TGEPSLLPDS PVGQLHASLL GLSQLLQPEG HHWETQQIPS LSPSQPWQRL LLRFKILRSL QAFVAVAARV FAHGAATLSP 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.
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Name :
IL 31 HumanDescription:
Interleukin-31 Human Recombinant
Interleukin 31, IL31, IL-31.
Product # :
CYT-625Price :
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Shipped at Room temp
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Description
IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.
Source
Escherichia Coli.
Formulation
The IL-31 (1mg/ml) was lyophilized with 20mM Phosphate buffer, 150mM NaCl pH-7.4.
Purity
Greater than 95.0% as determined by(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by its ability to activate STAT following receptor ligand interaction and found to be <5ng/ml, corresponding to a specific activity of 200,000 units.More Info
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Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis. -
Synonyms
Interleukin 31, IL31, IL-31.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-31 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IL-31 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT T.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KLF4 HumanDescription:
Kruppel-Like Factor 4 Human Recombinant
Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.
Product # :
PRO-891Price :
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Shipped with Ice Packs
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Description
KLF4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 545 amino acids (11-395) and having a molecular mass of 58.1 kDa.The KLF4 is fused to a 159 amino acid His-CaM Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KLF4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.
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Synonyms
Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MAHHHHHHMA DQLTEEQIAE FKEAFSLFDK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGYIS AAELRHVMTN LGEKLTDEEV DEMIREADID GDGQVNYEEF VQMMTAKGSM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV PPLHYQELMP PGSCMPEEPK PKRGRRSWPR KRTAT
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PhI p 1Description:
Pollen allergen Phl p 1 Recombinant
Pollen allergen Phl p 1, Allergen Phl p I, Phl p 1, PHLPI.
Product # :
PRO-2305Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Pollen allergen Phl p 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 29,516 Dalton. PhI p 1 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PhI p 1 protein solution is supplied in 20mM HEPES pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Pollen allergen Phl p 1 (PhI p 1) causes an allergic reaction in humans.
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Synonyms
Pollen allergen Phl p 1, Allergen Phl p I, Phl p 1, PHLPI.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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Molar extinction coefficient
46785; A280(1mg/ml)=1.699
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FGF23 HumanDescription:
Fibroblast Growth Factor-23 Human Recombinant
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Product # :
CYT-020Price :
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Shipped at Room temp
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Description
Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
More Info
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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
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Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
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Background
Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.
Mechanism
Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.Interactions
Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.Function
Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.Structure
FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.What is the molecular weight/Mw of FGF23 HUMAN Protein?
FGF23 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of FGF23 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF23 HUMAN Protein?
FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF23 HUMAN Protein?
The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.
What is the amino acid sequence of FGF23 HUMAN Protein?
MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.
What applications can FGF23 HUMAN Protein be used in?
FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF23 HUMAN Protein?
The endotoxin level is minimal, FGF23 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 5 HumanDescription:
Interleukin-5 Human Recombinant
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.
Product # :
CYT-212Price :
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Shipped at Room temp
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Description
Interleukin-5 Human Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing two 113 amino acids chains, and having a molecular mass of 26522.84 Dalton. The IL-5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 98.0% 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 the proliferation of TF-1 cells was found to be < 0.15ng/ml, corresponding to a Specific Activity of 6 x 106 IU/mg.More Info
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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
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Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL5 should be stored at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleikin-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ile-Pro-Thr-Glu.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Bcl XL Human, HisDescription:
B-Cell Lymphoma Extra Large Human Recombinant, His Tag
BclXL, Bcl-X(L), Bcl-XL.
Product # :
PRO-641Price :
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Description
Bcl-XL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-210.The Bcl-XL is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 10mM Tris-HCL pH-8, 1mM EDTA and 250mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein. -
Synonyms
BclXL, Bcl-X(L), Bcl-XL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bcl-XL although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-XL should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Suspend BclXL in 100?l of 0.5M Acetic acid, over night at 4°C.
Dilute 10 fold into selected buffer system.
Bcl-XL has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 33 RatDescription:
Interleukin-33 Rat Recombinant
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
Product # :
CYT-150Price :
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Shipped at Room temp
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Description
IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.4kDa.The IL 33 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine D10S cells is <0.5ng/ml, corresponding to a specific activity of >2,000,000units/mg.More Info
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Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
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Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IL-33 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SIQGTSLLTE SCALSTYNDQ SVSFVLENGC YVINVEDCGK NQEKDKVLLR YYESSFPAQS GDGVDGKKLM VNMSPIKDTD IWLNANDKDY SVELQKGDVS PPDQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE ENDESCNNIM FKLSKM
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Cor a 1.0103Description:
Major pollen allergen Cor a 1 Recombinant
Major pollen allergen Cor a 1 isoforms 5, 6, 11 and 16, Allergen Cor a I, Cor a 1, Cor a 1.0103.
Product # :
PRO-2285Price :
Quantity :
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Description
Recombinant Major pollen allergen Cor a 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,470 Dalton. Cor a 1.0103 purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Cor a 1.0103 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Major pollen allergen Cor a 1 (Cor a 1.0103) causes an allergic reaction in human. The Cor a 1 isoforms exhibit different antigenic and allergenic properties.
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Synonyms
Major pollen allergen Cor a 1 isoforms 5, 6, 11 and 16, Allergen Cor a I, Cor a 1, Cor a 1.0103.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
WB123 WuchereriaDescription:
Wb123 Wuchereria Bancrofti Recombinant
Product # :
PRO-2820Price :
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Shipped with Ice Packs
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Description
The E.Coli derived Recombinant Wuchereria Bancrofti Wb123 is a 43kDa protein which is fused to a His tag in N-terminus.
Source
Escherichia Coli.
Formulation
25mM K2CO3 and PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Background
One of the key antigens associated with Wuchereria bancrofti is Wb123, a protein that has emerged as a potential diagnostic marker for early infection and a target for vaccine development. Wb123 is a highly immunogenic protein that elicits a strong antibody response in individuals infected with Wuchereria bancrofti. Recombinant Wb123 is utilized in serological assays to detect specific IgG4 antibodies, which are indicative of active infection, particularly in the early stages before clinical symptoms manifest. Studies using rWb123 have demonstrated its high sensitivity and specificity, making it a valuable tool for diagnosing lymphatic filariasis and monitoring the effectiveness of mass drug administration (MDA) programs aimed at eliminating the disease.
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Specificity
Immunoassay.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C-PeptideDescription:
C-Peptide
Product # :
HOR-046Price :
Quantity :
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Shipped at Room temp
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Description
C-Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3020 Dalton and a Molecular formula of C129H211N35O48S .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized C-Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution C-Peptide should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized C-Peptide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-OH.
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Background
C-peptide, a small peptide derived from proinsulin, has garnered increasing attention in recent years for its multifaceted physiological functions and clinical significance, particularly in the context of diabetes mellitus. While initially considered a mere byproduct of insulin synthesis, research has revealed that C-peptide exerts unique biological effects, extending beyond glycemic control. This research endeavors to comprehensively investigate the roles of C-peptide, shedding light on its diverse functions and potential applications in diabetes management and other areas of healthcare.
The primary objective of this study is to unravel the mechanisms underlying the physiological actions of C-peptide. In vitro experiments using cellular and tissue models will be conducted to explore how C-peptide interacts with cellular receptors and signaling pathways. This includes investigations into its influence on insulin secretion, glucose uptake, and endothelial function. Understanding these mechanisms is essential for delineating the potential therapeutic applications of C-peptide.
The second objective is to assess the clinical relevance of C-peptide in diabetes management. Clinical trials involving individuals with type 1 and type 2 diabetes will be conducted to evaluate the effects of exogenous C-peptide administration on glycemic control, insulin sensitivity, and microvascular complications. These studies may provide valuable insights into the use of C-peptide as an adjunct therapy in diabetes treatment.
The third objective is to explore the broader implications of C-peptide in healthcare. Research will investigate the potential role of C-peptide in conditions beyond diabetes, such as its effects on cardiovascular health, neuroprotection, and wound healing. Understanding the multifunctional properties of C-peptide may open up new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of C-peptide, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may lead to innovative approaches for diabetes management and offer insights into the broader healthcare implications of C-peptide.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DNALI1 HumanDescription:
Dynein Axonemal Light Intermediate Chain 1 Human Recombinant
Dynein, Axonemal, Light Intermediate Chain 1, DJ423B22.5 (Axonemal Dynein Light Chain (Hp28)), Inner Dynein Arm Light Chain Axonemal, hp28, P28, Homolog Of Clamydomonas, Axonemal Dynein Light Intermediate Polypeptide 1, dJ423B22.5, Inner Dynein Arm, Homolog Of Clamydomonas, Dynein, Axonemal, Light Intermediate Polypeptide 1.
Product # :
PRO-1756Price :
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Description
DNALI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 34.2kDa. DNALI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DNALI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Dynein Axonemal Light Intermediate Chain1 also known as DNALI1 belongs to the inner dynein arm light chain family. DNALI1 take a dynamic role in flagellar motility. DNALI1 is the human homolog of the Chlamydomonas inner dynein arm gene, p28. The exactfunction of DNALI1 is not known yet, on the other hand, it is a potential candidate for immotile cilia syndrome. In addition it has been found that the following diseases: primary ciliary dyskinesia, and huntington's disease have been associated with DNALI1. Ultrastructural defects of the inner dynein arms are seen in patients with ICS. Immotile mutant strains ofChlamydomonas, biflagellated algae, show similar defects.
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Synonyms
Dynein, Axonemal, Light Intermediate Chain 1, DJ423B22.5 (Axonemal Dynein Light Chain (Hp28)), Inner Dynein Arm Light Chain Axonemal, hp28, P28, Homolog Of Clamydomonas, Axonemal Dynein Light Intermediate Polypeptide 1, dJ423B22.5, Inner Dynein Arm, Homolog Of Clamydomonas, Dynein, Axonemal, Light Intermediate Polypeptide 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVTANKA HTGQGSCWVA TLASAMIPPA DSLLKYDTPV LVSRNTEKRS PKARLLKVSP QQPGPSGSAP QPPKTKLPST PCVPDPTKQA EEILNAILPP REWVEDTQLW IQQVSSTPST RMDVVHLQEQ LDLKLQQRQA RETGICPVRR ELYSQCFDEL IREVTINCAE RGLLLLRVRD EIRMTIAAYQ TLYESSVAFG MRKALQAEQG KSDMERKIAE LETEKRDLER QVNEQKAKCE ATEKRESERR QVEEKKHNEE IQFLKRTNQQ LKAQLEGIIA PKK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DBI MouseDescription:
Diazepam Binding Inhibitor Mouse Recombinant
Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.
Product # :
PRO-2527Price :
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Description
DBI Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 12.4kDa. DBI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DBI protein solution (1mg/ml) contains Phosphate buffer saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DBI, also known as Acyl-CoA-binding protein isoform 2, is a diazepam binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.
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Synonyms
Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSQAEFD KAAEEVKRLK TQPTDEEMLF IYSHFKQATV GDVNTDRPGL LDLKGKAKWD SWNKLKGTSK ESAMKTYVEK VDELKKKYGI
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 10 Human, HisDescription:
Interleukin-10 Human Recombinant, His
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Product # :
CYT-486Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Interleukin-10 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 181 amino acids fragment (19-178) and having a total molecular mass of 20.94kDa with a 20 amino acids N-Terminal His tag. The IL-10 His-Tag protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-10 His is supplied in 20mM Tris-HCl pH-8 and 20% glycerol.
Purity
Greater than 95.0% by SDS-PAGE.
More Info
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Introduction
Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.
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Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 28A HumanDescription:
Interleukin-28A Human Recombinant
Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
Product # :
CYT-602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-28A human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 μm filtered solution containing no additives.
Purity
Greater than 85% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
IL-28A is distantly related to type I IFNs and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection. -
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 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.
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Solubility
It is recommended to reconstitute the lyophilized IL-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VPVAR LHGALPDARG CHIAQFKSLS PQELQAFKRAKDALEESLLL KDCRCHSRLF PRTWDLRQLQ VRERPMALEA ELALTLKVLE ATADTDPALV DVLDQPLHTL HHILSQFRAC IQPQPTAGPR TRGRLHHWLY RLQEAPKKES PGCLEASVTFNLFRLLTRDL NCVASGDLCV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
APOH HumanDescription:
Apolipoprotein-H Human
Beta-2-glycoprotein 1, Beta-2-glycoprotein I, Apolipoprotein H, Apo-H, B2GPI, Beta(2)GPI, Activated protein C-binding protein, APC inhibitor, Anticardiolipin cofactor, APOH, B2G1, BG, B2GP-1, B2 Glycoprotein-I.
Product # :
PRO-552Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human APOH produced in Human Plasma having a molecular mass of 50kDa and pI of 5.6-6.4. It’s a major phospholipid binding protein and an important component to measure in the assessment of anti-phospholipid syndrome. APOH is also more specific than anti-cardiolipin antibodies and its presence correlates better with thrombotic risk.
Source
Human Plasma.
Formulation
Lyophilized from 0.02M NH4HCO3.
Purity
Greater than 96.0%.
More Info
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Introduction
Apolipoprotein H (APOH) attaches to numerous kinds of negatively charged substances for instance heparin, phospholipids, and dextran sulfate. APOH prevents activation of the intrinsic blood coagulation cascade by attaching to phospholipids on the surface of damaged cells. APOH expressed by the liver and secreted in the plasma.
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Synonyms
Beta-2-glycoprotein 1, Beta-2-glycoprotein I, Apolipoprotein H, Apo-H, B2GPI, Beta(2)GPI, Activated protein C-binding protein, APC inhibitor, Anticardiolipin cofactor, APOH, B2G1, BG, B2GP-1, B2 Glycoprotein-I.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Human APOH although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized APOH in phosphate buffer, pH >7.0 containing 0.15M NaCl.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Calcitonin SalmonDescription:
Calcitonin Acetate Salmon
CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.
Product # :
HOR-262Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Calcitonin Acetate (Salmon) is a synthetic polypeptide of 32 amino acids in the same linear sequence that is found in calcitonin of salmon origin. The Molecular Formula is C145H240N44O48S2. Calcitonin Molecular Weight: 3431.9 Dalton.
Formulation
The calcitonin 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
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Introduction
Calcitonin (CT) is a peptide hormone produced by the parafollicular cells of the thyroid gland in mammals and by the ultimobranchial gland of birds and fish. Salmon calcitonin (sCT), which is more potent and longer lasting than human CT, has been used widely for the treatment of osteoporosis, paget's disease, hypercalcemic shock and chronic pain in terminal cancer patients. sCT is one of the many bioactive peptides that require C-terminal amidation for full biological activity.
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Synonyms
CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Calcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CGRP should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Calcitonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Calcitonin Acetate (Salmon) has an amino acid sequence of: Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NOV Human (260-357)Description:
Nephroblastoma Overexpressed (260-357 a.a.) Human Recombinant
Igfbp9, igfbp-9.
Product # :
CYT-1234Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The IGFBP9 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The IGFBP9 His-Tagged Fusion Protein, produced in E. coli, is a 18kDa protein containing 98 amino acid residues of the IGFBP9 Human, 260-357 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
Igfbp9, igfbp-9.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized IGFBP9 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Nephroblastoma Overexpressed (NOV) is a part of the CCN (CTGF/CYR61/NOV) family which takes an important part in tissue repair and cellular signaling, differentiation and growth. NOV takes part in angiogenesis, extracellular matrix remodeling and cellular adhesion. NOV is also involved in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and participates in both internal and external cell signaling. NOV is expressed in tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
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.