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1000 results found for “erythropoietin”
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Name :
PNC-27Description:
PNC-27
Product # :
HOR-038Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- HPLC, MS
Description
PNC-27 Synthetic is a single, non-glycosylated polypeptide chain containing 32 amino acids, having a molecular mass of 4031.72 Dalton and a Molecular formula of C188H293N53O44S.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
HPLC, MS
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PNC-27 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PNC-27 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 PNC-27 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-Pro-Pro-Leu-Ser-Gln-Glu-Thr-Phe-Ser-Asp-Leu-Trp-Lys-Leu-Leu-Lys-Lys-Trp-Lys-Met-Arg-Arg-Asn-Gln-Phe-Trp-Val-Lys-Val-Gln-Arg-Gly-OH
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Background
PNC-27, a promising anticancer peptide, has gained attention due to its selective cytotoxicity against cancer cells without harming normal cells. This paper aims to elucidate the biochemical characteristics of PNC-27 and explore its potential therapeutic applications in the field of oncology.
PNC-27, a novel anticancer peptide, holds great promise in the treatment of cancer due to its unique mechanism of action and selective cytotoxicity towards cancer cells (Goldberg et al., 2010). This paper seeks to delve into the biochemical attributes of PNC-27 and its therapeutic potential in cancer treatment.
Derived from the p53 tumor-suppressor protein, PNC-27 exhibits a unique binding affinity for the MDM-2 protein found in the membranes of cancer cells. This binding triggers membrane pore formation, leading to cell lysis and death, leaving normal cells unaffected (Goldberg et al., 2010).
Preclinical studies have highlighted the potential of PNC-27 in treating various types of cancers. Its ability to induce cell death in cancer cells without harming normal cells presents a promising direction for cancer therapeutics. For instance, studies have shown PNC-27 to be effective against lung and breast cancers (Hoshino et al., 2011; Sarafraz-Yazdi et al., 2010).
The promising potential of PNC-27 warrants further exploration in clinical trials to evaluate its efficacy and safety in humans. Furthermore, investigation into its synergistic effects with other cancer treatments could provide a more holistic approach to cancer therapeutics. In conclusion, PNC-27 presents an exciting avenue for cancer research, offering a novel and targeted approach to cancer treatment.
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 :
NEFL HumanDescription:
Neurofilament Light Human Recombinant
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2584Price :
Quantity :
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Shipped at Room temp
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Description
NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).
Source
Escherichia Coli.
Formulation
NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.
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 :
GHBP HumanDescription:
GHBP Human Recombinant
Product # :
CYT-238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GHBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids and having a molecular mass of 28107.01 Dalton. GHR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GHBP was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
GHBP is fully biologically active as evidenced by its ability of forming 2:1 complex with G.H.
More Info
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Introduction
GHBP is a transmembrane receptor for GH. Binding of GH to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the GH insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GHBP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP 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 GHBP 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
AFSGSEATAAILSRAPWSLQSVNPGLKTNS SKEPKFTKCRSPERETFSCHWTDEVHHGTK
NLGPIQLFYTRRNTQEWTQEWKECPDYVSA GENSCYFNSSFTSIWIPYCIKLTSNGGTVD
EKCFSVDEIVQPDPPIALNWTLLNVSLTGI HADIQVRWEAPRNADIQKGWMVLEYELQYK
EVNETKWKMMDPILTTSVPVYSLKVDKEYE VRVRSKQRNSGNYGEFSEVLYVTLPQMSQF
TCEEDFYF. -
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.6 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 GHBP 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.
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Name :
Ganirelix peptideDescription:
Ganirelix
Product # :
HOR-276Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ganirelix acetate is a synthetic decapeptide with high antagonistic activity against naturally occurring gonadotropin-releasing hormone (GnRH). Ganirelix acetate is derived from native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, 8, and 10 to form the following molecular formula of the peptide: N-acetyl-3-(2-napthyl)-D-alanyl-4-chloro-D-phenylalanyl-3-(3-pyridyl)-D-alanyl-L-seryl-L-tyrosyl-N 9 ,N 10 -diethyl- D-homoarginyl-L-leucyl-N 9 ,N 10 -diethyl-L-homoarginyl-L-prolyl-D-alanylamide acetate. The molecular weight for Ganirelix acetate is 1570.4 Dalton as an anhydrous free base.
Formulation
The Ganirelix hormone (0.5mg/ml) contains 0.1mg acetic acid and 23.5mg mannitol pH-5.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Ganirelix should be stored between 2°C- 8°C at all time. DO NOT FREEZE.
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Background
What is the molecular weight/Mw of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein has a total Mw of 1.57kDa.
What is the Purity of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GANIRELIX PEPTIDE Protein?
The biological functionality of GANIRELIX PEPTIDE Protein will be determined in the future.
What applications can GANIRELIX PEPTIDE Protein be used in?
GANIRELIX PEPTIDE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GANIRELIX PEPTIDE Protein?
The endotoxin level is minimal, GANIRELIX PEPTIDE 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 :
LysostaphinDescription:
Lysostaphin Recombinant
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
Product # :
ENZ-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without any additives.
Purity
98% as determined by RP-HPLC.
Biological Activity
Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C. Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.
More Info
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Introduction
Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.
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Synonyms
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.
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Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 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 RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.
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Specific Activity
Determined to be 3,540 units/mg.
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 :
TSH HumanDescription:
Thyroid Stimulating Hormone Human
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Product # :
HOR-001Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thyroid Stimulating Hormone Human produced in Human pituitary glands is an important indicator of thyroid function.
Source
Human pituitary glands
Formulation
Lyophilized from a concentrated solution containing 50mM ammonium bicarbonate.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.More Info
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Introduction
Thyroid-stimulating hormone (also known as TSH or thyrotropin) is a hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland which regulates the endocrine function of the thyroid gland.
TSH stimulates the thyroid gland to secrete the hormones thyroxine (T4) and triiodothyronine (T3). TSH production is controlled by a Thyrotropin Releasing Hormone, (TRH), which is manufactured in the hypothalamus and transported to the Anterior Pituitary gland, where it increases TSH production and release. Somatostatin is also produced by the hypothalamus, and has an opposite effect on the pituitary production of TSH, decreasing or inhibiting its release.
The level of Thyroid hormones (T3 and T4) in the blood have an additional effect on the pituitary release of TSH, When the levels of T3 and T4 are low, the production of TSH is increased, and conversely, when levels of T3 and T4 are high, then TSH production is decreased. This effect creates a regulatory negative feedback loop.
TSH is a glycoprotein and consists of two subunits, the alpha and the beta subunit.
The a (alpha) subunit is identical to that of human chorionic gonadotropin (HCG), luteinising hormone (LH), follicle-stimulating hormone (FSH).
The b (beta) subunit is unique to TSH, and therefore determines its function. -
Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSH 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 TSH 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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Background
What is the source or expression system of TSH HUMAN Protein?
Human pituitary glands
What is the Purity of TSH HUMAN Protein?
TSH HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of TSH HUMAN Protein?
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.
What applications can TSH HUMAN Protein be used in?
TSH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TSH HUMAN Protein?
The endotoxin level is minimal, TSH 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 :
GM-CSF Human, HisDescription:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, His Tag
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Product # :
CYT-477Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GMCSF Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids fragment (18-144) and having a molecular mass of 18.98kDa with an amino-terminal hexahistidine tag. GM-CSF Human Recombinant His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Granulocyte Macrophage Colony Stimulating Factor-His is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein has a total Mw of 18.98kDa.
What is the source or expression system of GM-CSF HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF HUMAN, HIS Protein?
The biological functionality of GM-CSF HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein is composed from 127 amino acids.
What applications can GM-CSF HUMAN, HIS Protein be used in?
GM-CSF HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF HUMAN, HIS Protein?
The endotoxin level is minimal, GM-CSF HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VEGF EquineDescription:
Vascular Endothelial Growth Factor Equine Recombinant
VEGF-A, VPF, glioma-derived endothelial cell mitogen.
Product # :
CYT-1200Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
VEGF Equine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 2 x 165 amino acids and having a total molecular mass of 38.6 kDa.The VEGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM Sodium Phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by HUVEC Proliferation is ≤ 10 ng/mL, corresponding to a specific activity of ≥ 1.0 x 10^5 units/mg.
More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
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Synonyms
VEGF-A, VPF, glioma-derived endothelial cell mitogen.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF Human 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 VEGF in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAPMAEGEHK THEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TAEFNITMQI MRIKPHQSQH IGEMSFLQHS KCECRPKKDK ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
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 :
ARF4 HumanDescription:
ADP-Ribosylation Factor 4 Human Recombinant
ADP-ribosylation factor 4, ARF4, ARF2.
Product # :
PRO-066Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARF4 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 204 amino acids (1-180 a.a.) and having a molecular mass of 23kDa. The ARF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF4 solution (0.5 mg/ml) in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ARF4 belongs to the ARF gene family whose members encode small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. The ARF proteins include five ARF proteins and eleven ARF-like proteins and constitute one family of the RAS superfamily. They are classified as class I, class II and class III; the ARF4 gene is a class II member. The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains 6 exons and 5 introns. The ARF4 gene is the most divergent member of the human ARFs.
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Synonyms
ADP-ribosylation factor 4, ARF4, ARF2.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMGLTIS SLFSRLFGKK QMRILMVGLD AAGKTTILYK LKLGEIVTTI PTIGFNVETV EYKNICFTVW DVGGQDRIRP LWKHYFQNTQ GLIFVVDSND RERIQEVADE LQKMLLVDEL RDAVLLLFAN KQDLPNAMAI SEMTDKLGLQ SLRNRTWYVQ ATCATQGTGL YEGLDWLSNE LSKR.
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 :
VEGF (121 a.a.) MouseDescription:
Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-574Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor-121 Mouse Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28.4 kDa.Recombinant Mouse VEGF-121 is a truncated version of Murine VEGF-165.The VEGF-121 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 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF-121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 VEGF-121 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
MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKRPR R.
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 :
EFNB3 Human, Sf9Description:
Ephrin- B3 Human Recombinant, Sf9
Ephrin B3, EPH-Related Receptor Transmembrane Ligand ELK-L3, Ephrin-B3, EPLG8, LERK8, Eph-Related Receptor Tyrosine Kinase Ligand 8, EPH-Related Receptor Tyrosine Kinase Ligand 8, LERK-8, EFL6, Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8.
Product # :
PRO-2381Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
EFNB3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 208 amino acids (28-226a.a.) and having a molecular mass of 23.0kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). EFNB3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.
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Synonyms
Ephrin B3, EPH-Related Receptor Transmembrane Ligand ELK-L3, Ephrin-B3, EPLG8, LERK8, Eph-Related Receptor Tyrosine Kinase Ligand 8, EPH-Related Receptor Tyrosine Kinase Ligand 8, LERK-8, EFL6, Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8.
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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.
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Amino Acid Sequence
ADPLSLEPVY WNSANKRFQA EGGYVLYPQI GDRLDLLCPR ARPPGPHSSP NYEFYKLYLV GGAQGRRCEA PPAPNLLLTC DRPDLDLRFT IKFQEYSPNL WGHEFRSHHD YYIIATSDGT REGLESLQGG VCLTRGMKVL LRVGQSPRGG AVPRKPVSEM PMERDRGAAH SLEPGKENLP GDPTSNATSR GAEGPLPPPS MPHHHHHH.
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 :
NRIP3 HumanDescription:
Nuclear Receptor-Interacting Protein 3 Human Recombinant
C11orf14, NY-SAR-105, Nuclear receptor-interacting protein 3, Sarcoma antigen NY-SAR-105, NRIP3.
Product # :
PRO-1384Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRIP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-241 a.a.) and having a molecular mass of 29.4kDa. NRIP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NRIP3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear Receptor-Interacting Protein (NRIP3)is a 241 amino acid protein which is encoded by a gene that maps to human chromosome 11.Diseases associated with NRIP3 include sarcoma, and acute myeloid leukemia.
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Synonyms
C11orf14, NY-SAR-105, Nuclear receptor-interacting protein 3, Sarcoma antigen NY-SAR-105, NRIP3.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFYSGLL TEGGRKETDM REAASLRQQR RMKQAVQFIH KDSADLLPLD GLKKLGSSKD MQPHNILQRR LMETNLSKLR SGPRVPWASK TNKLNQAKSE GLKKSEEDDM ILVSCQCAGK DVKALVDTGC LYNLISLACV DRLGLKEHVK SHKHEGEKLS LPRHLKVVGQ IEHLVITLGS LRLDCPAAVV DDNEKNLSLG LQTLRSLKCI INLDKHRLIM GKTDKEEIPF VETVSLNEDN TSEA.
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 :
BST1 HumanDescription:
Bone Marrow Stromal Cell Antigen 1 Human Recombinant
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.
Product # :
CYT-1071Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.
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Synonyms
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 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
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
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Background
The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine
Introduction
In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.
BST-1: A Versatile Player
BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.
Engineering a Cellular Conductor
With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.
Entering the Biological Stage
Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.
An Enthusiastic Applause for Results
Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.
Conclusion
The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST1 Protein?
BST1 Protein has a total Mw of 30.5kDa.
What is the source or expression system of BST1 Protein?
Sf9, Baculovirus cells.
What is the Purity of BST1 Protein?
BST1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BST1 Protein?
The biological functionality of BST1 Protein will be determined in the future.
What is the amino acid sequence of BST1 Protein?
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
What applications can BST1 Protein be used in?
BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BST1 Protein?
The endotoxin level is minimal, BST1 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.
- View Data Sheet
Name :
BST2 HumanDescription:
Bone Marrow Stromal Cell Antigen 2 Human Recombinant
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.
Product # :
CYT-059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.
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Synonyms
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
NPC-A-7. -
Physical Appearance
BST2 is supplied as a 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 MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
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Background
The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine
Introduction
As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.
BST-2: The Cellular Virtuoso
BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.
Engineering a Cellular Maestro
Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.
Stepping into the Biological Arena
Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.
A Standing Ovation for Results
Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.
Conclusion
The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST2 Protein?
BST2 Protein has a total Mw of 14.8kDa.
What is the source or expression system of BST2 Protein?
Escherichia Coli.
What is the Purity of BST2 Protein?
BST2 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of BST2 Protein?
The biological functionality of BST2 Protein will be determined in the future.
What is the amino acid sequence of BST2 Protein?
MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
What applications can BST2 Protein be used in?
BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BST2 Protein?
The endotoxin level is minimal, BST2 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.
- View Data Sheet
Name :
Super Leptin qA OvineDescription:
Super Leptin Antagonist Ovine Recombinant
Product # :
CYT-1245Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Ovine leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Ovine leptin antagonist 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.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, 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 Ala-Val-Pro-Ile-Arg.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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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 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.
- View Data Sheet
Name :
SCF HumanDescription:
Stem Cell Factor Human Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem Cell Factor Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% 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 Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor 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-Glu-Gly-Ile-Cys.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.52 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 Stem Cell Factor 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.
- View Data Sheet
Name :
MRPL13 HumanDescription:
Mitochondrial Ribosomal Protein L13 Human Recombinant
L13, L13A, L13mt, RPL13, RPML13, 39S ribosomal protein L13, mitochondrial, MRPL13.
Product # :
PRO-1404Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MRPL13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178 a.a.) and having a molecular mass of 23.1kDa. MRPL13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
MRPL13 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and assist in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit (MRPL13 is a 39S subunit protein) and have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. An additional difference between mammalian mitoribosomes and prokaryotic ribosomes is that the second contain a 5S rRNA. Among various species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology.
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Synonyms
L13, L13A, L13mt, RPL13, RPML13, 39S ribosomal protein L13, mitochondrial, MRPL13.
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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
MGSSHHHHHH SSGLVPRGSH MGSMSSFSRA PQQWATFARI WYLLDGKMQP PGKLAAMASI RLQGLHKPVY HALSDCGDHV VIMNTRHIAF SGNKWEQKVY SSHTGYPGGF RQVTAAQLHL RDPVAIVKLA IYGMLPKNLH RRTMMERLHL FPDEYIPEDI LKNLVEELPQ PRKIPKRLDE YTQEEIDAFP RLWTPPEDYR L.
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 :
SERPINA3Description:
Alpha-1 AntiChymotrypsin Human Recombinant
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-750Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
SERPINA3 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 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 3 HumanDescription:
Interleukin-3 Human Recombinant
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Product # :
CYT-210Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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
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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.
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Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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.
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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.
- View Data Sheet
Name :
CALB2 HumanDescription:
Calbindin-2 Human Recombinant
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
Product # :
PRO-401Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.
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Synonyms
Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.
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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
MGSSHHHHHH SSGLVPRGSH MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.
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 :
CALM2 HumanDescription:
Calmodulin-2 Human Recombinant
PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.
Product # :
PRO-618Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
Recombinant CALM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 16 kDa. CALM2 is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The CALM2 solution (1mg/ml) contains 20mM Tris-HCl, pH-7.5.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.
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Synonyms
PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.
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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
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK.
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 :
Flt3 Ligand PorcineDescription:
Flt3 Ligand Porcine Recombinant
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-1041Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Flt3-L 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
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
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Background
What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.
What is the source or expression system of FLT3 LIGAND PORCINE Protein?
Escherichia Coli.
What is the Purity of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.
What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
What applications can FLT3 LIGAND PORCINE Protein be used in?
FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
The endotoxin level is minimal, FLT3 LIGAND PORCINE 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.
- View Data Sheet
Name :
CDC123 HumanDescription:
Cell Division Cycle 123 Human Recombinant
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
Product # :
PRO-1463Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.
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Synonyms
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
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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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD
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 :
HaptoglobinDescription:
Haptoglobin Human Recombinant
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
Product # :
PRO-567Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Haptoglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing fusion protein with His tag and having a total Mw of 33 kDa (4 kDa His-tag).
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin, lung, and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury, and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system (generally the spleen). As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body, haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin, haptoglobin sequesters the iron inside hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis.
Haptoglobin consists of two A- and two B-chains, connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist (Hp 1-1, Hp 2-1, and Hp 2-2). Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active, and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, primary sclerosing cholangitis, susceptibility to idiopathic Parkinson's disease, and a reduced incidence of Plasmodium falciparum malaria. -
Synonyms
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Haptoglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Haptoglobin 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 Haptoglobin 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
L ILGGHLDAKG SFPWQAKMVS HHNLTTGATL INEQWLLTTA KNLFLNHSEN ATAKDIAPTL TLYVGKKQLV EIEKVVLHPN YSQVDIGLIK LKQKVSVNER VMPICLPSKD YAEVGRVGYV SGWGRNANFK FTDHLKYVML PVADQDQCIR HYEGSTVPEK KTPKSPVGVQ PILNEHTFCA GMSKYQEDTC YGDAGSAFAV HDLEEDTWYA TGILSFDKSC AVAEYGVYVK VTSIQDWVQK TIAEN
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.