Search: 973 results found for "General Transcription Factor"

Description:

Prolactin-Induced Protein Human

Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.

Product # :

CYT-779

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Description

The Prolactin-Induced Protein produced from Human Seminal Plasma has a molecular mass of 13.52kDa (calculated without glycosylation) containing 118 amino acid residues.

Source

Human Seminal Plasma.

Formulation

PIP protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Prolactin inducible protein (PIP) is a 17kDa glycoprotein existing in human seminal plasma. PIP is synthesized as a 146 amino acid long polypeptide exhibiting high sequence similarity with mouse submaxillary gland with a single glycosylation site. The precise biological functions of PIP are still ambiguous but various functions have been assigned to PIP due its existence at high concentration in biological fluids. PIP binds to various proteins such as fibrinogen, actin, keratin, myosin and tropomyosin. PIP is also expressed in pathological conditions of the mammary gland and in some exocrine tissues, such as the lacrimal, salivary and sweat glands. Due to PIP’s association with secretory cell differentiation, it has been used in diagnostic evaluation of tumors of breast, salivary gland, and skin.
Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. PIP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QDNTRKIIIK NFDIPKSVRP NDEVTAVLAV QTELKECMVV KTYLISSIPL QGAFNYKYTA CLCDDNPKTF YWDFYTNRTV QIAAVVDVIR ELGICPDDAA VIPIKNNRFY TIEILKVE.
Human Virus Test
Samples from each donor have been tested and found negative for HBsAg, HIV1+2, HCV, syphilis, aHBc, RRR.

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.

Description:

Erythropoietin Rat Recombinant

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

Product # :

CYT-1187

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Description

EPO Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-192 a.a) containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

EPO protein (1mg/ml) contains 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 TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

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Introduction
Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.
Synonyms
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
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
DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.
Background
What is the molecular weight/Mw of EPO Protein?
EPO Protein has a total Mw of 19.6kDa.

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

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

What is the Biological Activity of EPO Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

What is the amino acid sequence of EPO Protein?
DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

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

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

Description:

Leptin Human Recombinant, His Tag

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-287

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Description

Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.
Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

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.

Description:

Growth Hormone Bovine Recombinant

BGH, BST, rBGH, rBST, Bovine Somatotropin, Bovine GH, Growth hormone, GH1.

Product # :

CYT-636

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Description

Growth Hormone Bovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.8 kDa. The GH Bovine Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Bovine Growth Hormone protein was lyophilized from a concentrated (1mg/ml) solution with 4.5mM NaHCO3 adjusted to pH 8-9.

Purity

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

Biological Activity

The activity as determined by the PDFP13B9 cells stably transfected with rabbit GH receptors. Bovine GH is also capable of forming a 1:2 complex with the recombinant ovine growth hormone receptor extracellular domain (ECD).

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
BGH, BST, rBGH, rBST, Bovine Somatotropin, Bovine GH, Growth hormone, GH1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bovine Growth Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH Bovine 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 Bovine Growth Hormone in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences.

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.

Description:

Retinol Binding Protein-7 Human Recombinant

Retinoid-binding protein 7, Cellular retinoic acid-binding protein 4, CRABP4, CRBP4, Cellular retinoic acid-binding protein IV, CRABP-IV, RBP7, MGC70641.

Product # :

CYT-023

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Shipped with Ice Packs

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Description

RBP7 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-134 a.a.) and having a molecular mass of 17.6kDa. The RBP7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RBP7 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
RBP7 is a member of a superfamily of small cytoplasmic proteins which interact with hydrophobic ligands. RBP7 is cytoplasmic protein which, like CRBP I and CRBP II, forms ?-barrel structures and participates in the intracellular transport of retinol. RBP7 is a newly identified cellular retinol carrier, which is expressed in the kidney, heart and transverse colon in humans.
Synonyms
Retinoid-binding protein 7, Cellular retinoic acid-binding protein 4, CRABP4, CRBP4, Cellular retinoic acid-binding protein IV, CRABP-IV, RBP7, MGC70641.
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 MPADLSGTWT LLSSDNFEGY MLALGIDFAT RKIAKLLKPQ KVIEQNGDSF TIHTNSSLRN YFVKFKVGEE FDEDNRGLDN RKCKSLVIWD NDRLTCIQKG EKKNRGWTHW IEGDKLHLEM FCEGQVCKQT FQRA.

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.

Description:

Interleukin-2 Porcine Recombinant

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

Product # :

CYT-397

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Description

Interleukin2 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 15217 Dalton. The IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 10⁶IU/mg.

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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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL 2 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSTKNT KKQLEPLLLD LQLLLKEVKN YENADLSRML TFKFYMPKQA TELKHLQCLV EELKALEGVL NLGQSKNSDS ANIKESMNNI NVTVLELKGS ETSFKCEYDD ETVTAVEFLN KWITFCQSIY STLT.
Background
What is the molecular weight/Mw of IL 2 PORCINE Protein?
IL 2 PORCINE Protein has a total Mw of 15.2kDa.

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

What is the Purity of IL 2 PORCINE Protein?
IL 2 PORCINE Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 PORCINE Protein?
The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 106 IU/mg.

What is the amino acid sequence of IL 2 PORCINE Protein?
APTSSSTKNT KKQLEPLLLD LQLLLKEVKN YENADLSRML TFKFYMPKQA TELKHLQCLV EELKALEGVL NLGQSKNSDS ANIKESMNNI NVTVLELKGS ETSFKCEYDD ETVTAVEFLN KWITFCQSIY STLT.

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

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

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

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

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

Description:

ProInsulin C-Peptide Analogue Human Recombinant

Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

Product # :

CYT-1120

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Shipped at Room temp

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Description

ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin 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:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized ProInsulin C-Peptide Analogue in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

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.

Description:

Leptin Bovine Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-502

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Interleukin-6 Human Recombinant

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

Product # :

CYT-213

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
Synonyms
B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-6 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Val-Pro-Pro.
Background
What is the molecular weight/Mw of IL 6 HUMAN Protein?
IL 6 HUMAN Protein has a total Mw of 21kDa.

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

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

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

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

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

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

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

Where can I order bulk mg quantities of IL 6 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-6 as a Reference Standard.

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

Description:

Interleukin-11 Human Recombinant

AGIF, Adipogenesis inhibitory factor, IL-11.

Product # :

CYT-214

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19256.29 Dalton. The IL-11 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 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 murine 7TD1 was found to be < 10ng/ml, corresponding to a Specific Activity of 100,000 IU/mg.

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Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
Synonyms
AGIF, Adipogenesis inhibitory factor, IL-11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of IL11 HUMAN Protein?
IL11 HUMAN Protein has a total Mw of 19.25kDa.

What is the source or expression system of IL11 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL11 HUMAN Protein?
IL11 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL11 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be < 10ng/ml, corresponding to a Specific Activity of 100,000 IU/mg.

What is the amino acid sequence of IL11 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.

What applications can IL11 HUMAN Protein be used in?
IL11 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL11 HUMAN Protein?
The endotoxin level is minimal, IL11 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL11 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL11 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.95 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-11 as a Reference Standard.

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

Description:

Pegylated Rat Leptin Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-592

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Description

Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, 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.

Description:

Interleukin-2 Human Recombinant

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

Product # :

CYT-209

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa. The IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2μm filtered concentrated solution (1.0mg/ml) in PBS, pH 5.0.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x10⁷IU/mg.

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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), Lymphokine, IL-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-2 in sterile distilled water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.
Background
IL 2 HUMAN: A Vital Tool for Advancing Immunotherapy Research
IL 2 HUMAN refers to the human form of Interleukin-2, a critical cytokine in the immune system. This protein is crucial for the growth and activity of T and B lymphocytes, the cells responsible for the body's immune defense against infections.
By promoting the growth of these cells, IL 2 plays a vital role in maintaining and activating the immune response.
Production and Characteristics
Typically, IL 2 is produced through recombinant DNA technology using E. coli bacteria. This method allows for creating large quantities of pure and functional IL 2 protein.
The product appears as a sterile, white lyophilized powder that is non-glycosylated and consists of 133 amino acids with a molecular mass of approximately 15.4 kDa.
Reconstituting IL-2 Human for Laboratory Use
To dissolve the lyophilized IL-2 effectively, it should be reconstituted with sterile distilled water to achieve a minimum 100µg/ml concentration. This makes the protein readily usable for further experimental procedures.
Moreover, the concentration allows for easy adjustment in solubility and ensures optimal conditions for the protein's activity in various research setups. Proper dissolution and storage are crucial to maintain the protein's functionality and stability.
Storage and Stability
The stability of IL 2 is dependent on its storage conditions. When lyophilized, it can remain stable at room temperature for up to three weeks, but for long-term storage, it should be kept desiccated below -18°C.
Once reconstituted, IL 2 should be used within a week if kept at 4°C, or it can be stored at below -18°C for future use. It's important to avoid freeze-thaw cycles, which can degrade the protein.
Purity and Biological Activity
IL 2 HUMAN's purity is generally greater than 97%, confirmed by reverse-phase high-performance liquid chromatography (RP-HPLC) and SDS-PAGE analyses.
Its biological activity is evaluated by its ability to stimulate the proliferation of murine CTLL-2 cells, with an effective dose (ED50) typically less than 0.1 ng/ml. This indicates a very high specific activity, making it highly potent and effective in research settings.
Applications in Research
IL 2 is used extensively in research, particularly in studies focusing on the immune system, autoimmune diseases, and cancer. Furthermore, its role in T-cell growth and function makes it invaluable for developing new therapeutic strategies and understanding immune response mechanisms.
Important Considerations
It is important to remember that IL 2, like all cytokines used in research, is intended for laboratory use only. This protein is not suitable for drug, food, or cosmetic applications. Proper handling and usage instructions must be followed to ensure safety and efficacy in research environments.
Essentially, IL 2 HUMAN is a vital tool in immunological research, offering insights into the complex workings of the immune system and providing avenues for potential therapeutic developments. The careful production, handling, and storage of IL 2 are crucial for its effective use in laboratory settings.
What is the molecular weight/Mw of IL 2 HUMAN Protein?
IL 2 HUMAN Protein has a total Mw of 15.4kDa.

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

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

What is the Biological Activity of IL 2 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.

What is the amino acid sequence of IL 2 HUMAN Protein?
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

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

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

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

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

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

Description:

Leptin Mouse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-351

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

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source
formulation
purity
biological activity
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Description

Leptin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa. The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The mouse Leptin was lyophilized from a concentrated (1mg/ml) solution containing 0.0045mM NaHCO3.

Purity

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

Biological Activity

Biological activity of Mouse Leptin is performed by including proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

More Info

Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH-8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Interleukin-3 Human Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-210

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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biological activity
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Description

Interleukin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.3 mg/ml of NaHCO3.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

More Info

Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.
Background
What is the molecular weight/Mw of IL3 HUMAN Protein?
IL3 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of IL3 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL3 HUMAN Protein?
IL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

What is the amino acid sequence of IL3 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.

What applications can IL3 HUMAN Protein be used in?
IL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 HUMAN Protein?
The endotoxin level is minimal, IL3 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL3 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.84 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-3 as a Reference Standard.

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

Description:

Leptin Ovine Recombinant, MTS tag

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-531

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Ovine MTS tagged although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.02% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Leu-Leu-Pro.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Leptin Ovine Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-239

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Ovine as a Reference Standard.

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

Description:

Immature Colon Carcinoma Transcript 1 Human Recombinant

DS-1, DS1, Peptidyl-tRNA hydrolase ICT1 mitochondrial, Digestion substraction 1, Immature colon carcinoma transcript 1 protein, ICT1.

Product # :

PRO-1303

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

ICT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 22.8kDa. ICT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ICT1 protein solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol, 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Immature Colon Carcinoma Transcript 1 (ICT1) functions as a codon-independent translation release factor that has lost all stop codon specificity and leads the termination of translation in mitochondrion in case of abortive elongation. The mature colon epithelium has 3 differentiated cell types which arise from a multipotent stem cell. ICT1 is involved in the hydrolysis of peptidyl-tRNAs which have been prematurely terminated and consequently in the recycling of stalled mitochondrial ribosomes. Digression from the normal maturation pathway by neoplastic transformation is assumed to originate in stem cells or their early descendants.
Synonyms
DS-1, DS1, Peptidyl-tRNA hydrolase ICT1 mitochondrial, Digestion substraction 1, Immature colon carcinoma transcript 1 protein, ICT1.
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 MGSLHKQKDG TEFKSIYSLD KLYPESQGSD TAWRVPNGAK QADSDIPLDR LTISYCRSSG PGGQNVNKVN SKAEVRFHLA TAEWIAEPVR QKIAITHKNK INRLGELILT SESSRYQFRN LADCLQKIRD MITEASQTPK EPTKEDVKLH RIRIENMNRE RLRQKRIHSA VKTSRRVDMD.

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.

Description:

Corticotropin Releasing Hormone Human Recombinant

CRF, Corticotropin-Releasing Factor.

Product # :

HOR-053

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The CRH Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CRH His-Tagged Fusion Protein, produced in E. coli, is a 21kDa protein containing 154 amino acid residues of the CRH Human, 43-196 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

Synonyms
CRF, Corticotropin-Releasing Factor.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized CRH at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Corticotropin-Releasing Hormone (CRH) is a neuropeptide which regulates the body's response to stress. CRH stimulates the release of ACTH from the pituitary gland which triggers the adrenal glands to produce cortisol. CRH takes part in the hypothalamic-pituitary-adrenal axis which controls the production of cortisol and more various glucocorticoids. CRH is synthesized in different tissues such as the brainstem, hypothalamus and peripheral organs.
What is the molecular weight/Mw of CRH HUMAN Protein?
CRH HUMAN Protein has a total Mw of 21kDa.

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

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

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

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

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

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

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

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

Description:

Interleukin-3, Mouse Anti-Human

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

ANT-106

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Formulation

1mg/ml in PBS (after reconstitution).

More Info

Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-3.
Ig Subclass
Mouse Ig.
Clone
hIL3-E2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Immunohistochemistry.
Titer
By direct ELISA, 1:1,000 dilution will yield 0.2 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion Exchange.

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.

Description:

Insulin (20-110 a.a) Human Recombinant

Product # :

CYT-1237

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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Description

The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 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

Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Insulin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.

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.

Description:

Pegylated Mouse Leptin Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-591

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry. Since its enlarged hydrodymanic volume Pegylated Leptin runs on SDS-PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

Source

Escherichia Coli.

Formulation

The mouse Leptin was lyophilized from a concentrated (0.65mg/ml) solution containing 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated mouse Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated mouse Leptin in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5 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.

Description:

Leptin Clone PAT7E10AT, Mouse Anti Human

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

ANT-690

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Formulation

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

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human Leptin mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Leptin amino acids 22-167 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT7E10AT.
Applications
Leptin antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Leptin antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

Description:

Interleukin-10, Mouse Anti-Human

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

ANT-112

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-10.
Ig Subclass
Mouse IgG1.
Clone
NYR-HIL10.
Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion excahnge.

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.

Description:

UL16 Binding Protein 1 Human Recombinant

UL16 Binding Protein 1, Retinoic Acid Early Transcript 1I, alcan-beta, NKG2D Ligand 1, NKG2DL1, RAET1I, N2DL-1.

Product # :

CYT-166

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

ULBP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (26-216) and having a molecular mass of 25.0 kDa. ULBP1 is fused to a 25 amino acid His-tag at N-terminus AND purified by using conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The ULBP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 30% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ULBP1 together with at least ULBP2 and ULBP3, is ligand for the NKG2D receptor. ULBPs stimulate various signaling pathways in primary NK cells, which result in cytokines and chemokines production. In CMV infected cells, ULBP1 cooperates with soluble CMV glycoprotein UL16 to inhibit the interaction with the NKG2D receptor providing a mechanism by which CMV infected cells escape the immune system. Additionally, UL16 retains ULBP1 to the ER and cis-Golgi apparatus to prevent it from reaching cell surface.
Synonyms
UL16 Binding Protein 1, Retinoic Acid Early Transcript 1I, alcan-beta, NKG2D Ligand 1, NKG2DL1, RAET1I, N2DL-1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGWVDT HCLCYDFIIT PKSRPEPQWC EVQGLVDERP FLHYDCVNHK AKAFASLGKK VNVTKTWEEQ TETLRDVVDF LKGQLLDIQV ENLIPIEPLT LQARMSCEHE AHGHGRGSWQ FLFNGQKFLL FDSNNRKWTA LHPGAKKMTE KWEKNRDVTM FFQKISLGDC KMWLEEFLMY WEQMLDPTKP PSLAPG

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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