Search: 1000 results found for "procalcitonin"

Description:

Parathyroid Hormone (1-84) N15 Labeled Human Recombinant

Parathyrin, PTH, Parathormone.

Product # :

HOR-002

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures.
Synonyms
Parathyrin, PTH, Parathormone.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Parathormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.

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

Description:

LIGHT Human Recombinant

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

Product # :

CYT-1202

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

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

Source

Escherichia Coli.

Formulation

TNFSF14 solution contains PBS & 25mM K2CO3.

Purity

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

More Info

Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGPAGSWEQL IQERRSHEVN PAAHLTGANS SLTGSGGPLL WETQLGLAFL RGLSYHDGAL VVTKAGYYYI YSKVQLGGVG CPLGLASTIT HGLYKRTPRY PEELELLVSQ QSPCGRATSS SRVWWDSSFL GGVVHLEAGE KVVVRVLDER LVRLRDGTRS YFGAFMV

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

Description:

Mouse Anti Human Troponin I Type 1 Paired

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

Product # :

ANT-724

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
formulation
purity
More Info
Citations

Description

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

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

Formulation

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

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

Purity

Greater than 95%.

More Info

Introduction
Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.
Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Applications
Lateral flow immunoassay.
Type
Mouse Anti Human Monoclonal.
Purification Method
Purified monoclonal IgG by protein A chromatography.

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

Description:

Cardiac Troponin-I Human

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

Product # :

PRO-2788

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

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

Source

Human heart tissue.

Formulation

TNNI3 was lyophilized from 0.01M HCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

More Info

Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.
While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.
The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.
The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.

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

Description:

Progranulin Human Recombinant

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

Product # :

CYT-524

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

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

Source

HEK 293 cells.

Formulation

The protein contains 1xPBS.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

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

More Info

Introduction
A 88-kDa progranulin, also called proepithelin and PC cell-derived growth factor, is a single precursor protein of granulins which are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. Granulins are a variety of active, 6 kDa peptides and named granulin A (epithelin 1), granulin B (epithelin 2), granulin C, etc. Both the peptides and intact progranulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.
Synonyms
GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Progranulin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PGRN should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Progranulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

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

Product # :

CMV-218

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

More Info

Introduction
CMV is part of the Betaherpesvirinae subfamily of Herpesviridae; including herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses has the common ability to stay latentover long periods of time. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
Stability
CMV Pp65 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
CMV Pp65 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.
Specificity
Immunoreactive with sera of CMV-infected individuals.
Purification Method
CMV Pp65 was purified by proprietary chromatographic technique.

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

Description:

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

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

Product # :

CHM-349

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

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

Source

Pichia Pastoris.

Formulation

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

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

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

More Info

Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.
When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein has a total Mw of 9kDa.

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

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

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

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

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

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

Who supplies recombinant CXCL8 HUMAN, PICHIA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL8 HUMAN, PICHIA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Thyroglobulin Human, Biotinylated

Thyroglobulin, TGN, AITD3, TG.

Product # :

PRO-2563

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

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

Source

Native, Isolated from human thyroid glands.

Formulation

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

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.
Synonyms
Thyroglobulin, TGN, AITD3, TG.
Physical Appearance
Sterile Filtered solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

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

Description:

Cystatin-C Mouse Recombinant, Active

Cystatin-C, Cystatin-3, Cst3, CST3

Product # :

PRO-2433

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

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

More Info

Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
Synonyms
Cystatin-C, Cystatin-3, Cst3, CST3
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH

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

Description:

Interleukin-1 Alpha Porcine Recombinant

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

Product # :

CYT-396

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.
Background
What is the molecular weight/Mw of IL1A PORCINE Protein?
IL1A PORCINE Protein has a total Mw of 18kDa.

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

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

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

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

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

What is the endotoxin level for IL1A PORCINE Protein?
The endotoxin level is minimal, IL1A PORCINE Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.

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:

IL-6 Soluble Receptor Human Recombinant, Sf9

IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2, Membrane glycoprotein 80, gp80, IL-6R, MGC104991.

Product # :

CYT-1077

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
SDS-PAGE
Citations

Description

sIL6R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-365 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 355 amino acids and having a molecular mass of 39.6kDa.sIL6R purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

sIL6R protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using M1 mouse myeloid leukemia cells. The ED50 range ≤ 20 ng/ml with Human IL-6.

SDS-PAGE

More Info

Introduction
The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.
Synonyms
IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2, Membrane glycoprotein 80, gp80, IL-6R, MGC104991.
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
ADPLAPRRCP AQEVARGVLT SLPGDSVTLT CPGVEPEDNA TVHWVLRKPA AGSHPSRWAG MGRRLLLRSV QLHDSGNYSC YRAGRPAGTV HLLVDVPPEE PQLSCFRKSP LSNVVCEWGP RSTPSLTTKA VLLVRKFQNS PAEDFQEPCQ YSQESQKFSC QLAVPEGDSS FYIVSMCVAS
SVGSKFSKTQ TFQGCGILQP DPPANITVTA VARNPRWLSV TWQDPHSWNS SFYRLRFELR YRAERSKTFT TWMVKDLQHH CVIHDAWSGL RHVVQLRAQE EFGQGEWSEW SPEAMGTPWT ESRSPPAENE VSTPMQALTT NKDDDNILFR DSANATSLPV QDSSSVPLPH HHHHH
Background
What is the molecular weight/Mw of SIL 6R HUMAN, SF9 Protein?
SIL 6R HUMAN, SF9 Protein has a total Mw of 39.6kDa.

What is the source or expression system of SIL 6R HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of SIL 6R HUMAN, SF9 Protein?
SIL 6R HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of SIL 6R HUMAN, SF9 Protein?
Measured by its ability to inhibit proliferation using M1 mouse myeloid leukemia cells. The ED50 range ≤ 20 ng/ml with Human IL-6.

What is the amino acid sequence of SIL 6R HUMAN, SF9 Protein?
ADPLAPRRCP AQEVARGVLT SLPGDSVTLT CPGVEPEDNA TVHWVLRKPA AGSHPSRWAG MGRRLLLRSV QLHDSGNYSC YRAGRPAGTV HLLVDVPPEE PQLSCFRKSP LSNVVCEWGP RSTPSLTTKA VLLVRKFQNS PAEDFQEPCQ YSQESQKFSC QLAVPEGDSS FYIVSMCVAS
SVGSKFSKTQ TFQGCGILQP DPPANITVTA VARNPRWLSV TWQDPHSWNS SFYRLRFELR YRAERSKTFT TWMVKDLQHH CVIHDAWSGL RHVVQLRAQE EFGQGEWSEW SPEAMGTPWT ESRSPPAENE VSTPMQALTT NKDDDNILFR DSANATSLPV QDSSSVPLPH HHHHH.
What applications can SIL 6R HUMAN, SF9 Protein be used in?
SIL 6R HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for SIL 6R HUMAN, SF9 Protein?
The endotoxin level is minimal, SIL 6R HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant SIL 6R HUMAN, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of SIL 6R HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

IFN-Alpha 2a Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.

Product # :

CYT-204

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

IFN Alpha Human 2a Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine.The Interferon-alpha-2a gene was obtained from human leukocytes.The IFNA2A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized without additives.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

More Info

Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNA-2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha-2a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein has a total Mw of 19.2kDa.

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

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

What is the Biological Activity of IFN A 2A HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

What is the amino acid sequence of IFN A 2A HUMAN Protein?
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.

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

What is the endotoxin level for IFN A 2A HUMAN Protein?
The endotoxin level is minimal, IFN A 2A HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 IFN-a 2a 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-4 Porcine Recombinant

BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

Product # :

CYT-1098

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Interleukin-4 Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 110 amino acids and having a molecular mass of 12.7kDa. IL-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered 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 TF-1 cell proliferation is 0.504ng/ml corresponding to a specific activity which is 2.0 x 10^6 units/mg.

More Info

Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which contributes to various overlapping roles of this cytokine and IL13. STAT6, a signal transducer and activator of transcription plays a main role in mediating the immune regulatory signal of this cytokine. IL4, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are regulated co-ordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-4 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 IL-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHKCDITLQE IIKTLNILTA RKNSCMELPV TDVFAAPENT TEKETFCRAS TVLRHIYRHH TCMKSLLSGL DRNLSSMANM TCSVHEAKKS TLKDFLERLK TIMKEKYSKC.
Background
What is the molecular weight/Mw of IL 4 PORCINE Protein?
IL 4 PORCINE Protein has a total Mw of 12.7kDa.

What is the source or expression system of IL 4 PORCINE Protein?
Escherichia Coli.

What is the Purity of IL 4 PORCINE Protein?
IL 4 PORCINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 PORCINE Protein?
The ED50, as determined by TF-1 cell proliferation is 0.504ng/ml corresponding to a specific activity which is 2.0 x 10^6 units/mg.

What is the amino acid sequence of IL 4 PORCINE Protein?
MHKCDITLQE IIKTLNILTA RKNSCMELPV TDVFAAPENT TEKETFCRAS TVLRHIYRHH TCMKSLLSGL DRNLSSMANM TCSVHEAKKS TLKDFLERLK TIMKEKYSKC.

What applications can IL 4 PORCINE Protein be used in?
IL 4 PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 PORCINE Protein?
The endotoxin level is minimal, IL 4 PORCINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 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 4 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:

Candida Albicans Phospholipase B1 Recombinant

Product # :

PRO-2809

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Recombinant Candida Albicans Phospholipase B1 (24-526 a.a) produced in E. coli having a Mw of 52kDa. C.Albicans PLB1 is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Phosphate buffer and 25mM K2CO3.

Purity

Protein is >90% pure as determined by 10% PAGE (coomassie staining).

More Info

Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Background
Potential as a Therapeutic Target:
Understanding the role of PLB1 in fungal pathogenesis opens avenues for developing novel antifungal strategies. Inhibiting PLB1 activity could potentially render C. albicans less virulent and susceptible to host immune defenses. Recombinant Candida Albicans Phospholipase B1 studies play a critical role in identifying and characterizing potential inhibitors that could form the basis for antifungal drug development.
Challenges and Future Directions:
While the potential of Recombinant Candida Albicans Phospholipase B1 in antifungal research is promising, challenges persist. Fine-tuning its applications, deciphering its role in different infection scenarios, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, understanding the interplay between PLB1 and other virulence factors in C. albicans pathogenesis remains an active area of investigation.
Recombinant Candida Albicans Phospholipase B1 emerges as a key player in the intricate dance between the fungus and its human host. Its structural insights, enzymatic activities, and implications in host-pathogen interactions position it as a central focus in the exploration of C. albicans virulence. As researchers continue to unravel the molecular intricacies of PLB1, they not only deepen our understanding of fungal pathogenesis but also pave the way for transformative advancements in antifungal drug development, shaping the future of precision medicine in the realm of fungal infections.

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:

Mouse Anti Human Troponin I Type 3 Paired

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

Product # :

ANT-664

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
formulation
purity
More Info
Citations

Description

TNNI3 Paired antibodies, coating and conjugating are used for lateral flow immunoassay. Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).

Formulation

*Cardiac Troponin-I coating antibody (5mg/1ml) contains 50 mM Na-citrate, pH 6.0, 0.9 % NaCl and 0.095 % NaN3 as a preservative.

* Cardiac Troponin-I conjugating antibody (1mg/1ml) contains 50 mM Na-citrate, pH 6.0, 0.9 % NaCl and 0.095 % NaN3 as a preservative.

Purity

Greater than 95%.

More Info

Introduction
Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI is acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and is exclusively expressed in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).
Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Physical Appearance
2 vials of sterile filtered clear colorless solution.
Stability
Cardiac Troponin-I although stable at 4°C for 1 week, should be stored 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.
Applications
Lateral flow immunoassay.
Type
Mouse Anti Human Monoclonal.
Purification Method
Purified monoclonal IgG by protein A chromatography.

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

Description:

Interleukin-6 Clone PAT1F10AT, Mouse Anti Human

IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

Product # :

ANT-540

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

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

More Info

Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
Synonyms
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human IL-6, clone PAT1F10AT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL-6 protein 30-212 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT1F10AT.
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Background
Research Paper on Interleukin-6 Clone PAT1F10AT, Mouse Anti-Human
Abstract:
Interleukin-6 (IL-6) Clone PAT1F10AT, a Mouse Anti-Human monoclonal antibody, plays a pivotal role in deciphering the complexities of immune modulation. This research paper provides an insightful exploration of its molecular attributes and its profound implications in immunological research. We examine its interactions, functions, and synonyms, including DIF, TNFA, and TNFSF2, shedding light on its significance in understanding immune responses.
Introduction:
IL-6 Clone PAT1F10AT, a Mouse Anti-Human antibody, has emerged as a cornerstone in immunology research. This paper delves into its unique characteristics and its critical role in unraveling immune mechanisms.
Molecular Precision and Specificity:
The exceptional affinity and specificity of IL-6 Clone PAT1F10AT for human IL-6 distinguish it as an invaluable tool for immunodetection and functional studies. Its targeted binding facilitates accurate identification of IL-6 in various experimental contexts.
Unveiling Immune Dynamics:
IL-6 is a central player in immune orchestration, and IL-6 Clone PAT1F10AT offers a window into its world. By investigating its involvement in immune responses, inflammation, and signaling pathways, researchers gain insights into immune regulation.
Synonyms and Interactions:
Understanding IL-6 synonyms, such as DIF, TNFA, and TNFSF2, underscores its intricate web of interactions. IL-6 Clone PAT1F10AT's ability to decipher these connections enhances our understanding of cytokine-mediated immune modulation.
Disease Implications and Therapeutic Avenues:
With its relevance in diseases like autoimmune disorders and inflammatory conditions, IL-6 Clone PAT1F10AT assumes significance in disease-focused investigations. It enables researchers to dissect disease mechanisms and evaluate potential therapeutic interventions.
Clinical Utility and Diagnostic Precision:
IL-6 Clone PAT1F10AT's utility transcends research settings, finding application in clinical diagnostics. Its role in immunoassays facilitates accurate disease diagnosis and monitoring, contributing to improved patient management.
Conclusion:
In the realm of immunology, IL-6 Clone PAT1F10AT stands as a potent ally in unraveling immune intricacies. Its molecular precision, diverse functions, and potential therapeutic implications make it a cornerstone in advancing our understanding of immune responses and diseases.
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
IL-6 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:

Parathyroid Hormone (7-84) Human Recombinant

Parathyrin, PTH, Parathormone.

Product # :

HOR-011

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. The PTH (7-84) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

More Info

Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Synonyms
Parathyrin, PTH, Parathormone.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PTH (7-84) although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTH (7-84) should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PTH (7-84) in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.

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:

Protein Kinase C Iota Human Recombinant

DXS1179E, nPKC-iota, PKCI, aPKC-lambda/iota, PRKC-lambda/iota, PRKCL, Protein kinase C iota type, Protein Kinase C iota, Atypical protein kinase C-lambda/iota, PRKCI.

Product # :

PKA-132

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PRKCI Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (1-596 a.a) containing a total of 602 amino acids, having a molecular mass of 69kDa. PRKCI is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The PRKCI solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
PRKCI, AKAPKC iota, is part of serine/threonine protein kinases family. It takes a key regulatory role in a number of cellular functions including hormone secretion,cell growth differentiation, and gene expression. It is involved in cell polarization processes and the formation of epithelial tight junctions.This protein kinase is calcium-independent and phospholipid-dependent. It is also implicated in the activation of several signal-pathways such as Ras, and NF-kappa-B, c-Src pathways.
Synonyms
DXS1179E, nPKC-iota, PKCI, aPKC-lambda/iota, PRKC-lambda/iota, PRKCL, Protein kinase C iota type, Protein Kinase C iota, Atypical protein kinase C-lambda/iota, PRKCI.
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
MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPQEPV MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECVHHHH HH

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:

Protein Kinase IFN Double Stranded RNA Activator Human Recombinant

Interferon-inducible double-stranded RNA-dependent protein kinase activator A, Protein Kinase IFN Double Stranded RNA Activator, PKR-associated protein X, PKR-associating protein X, Protein activator of the interferon-induced protein kinase, Protein kinase, interferon-inducible double-stranded RNA-dependent activator, PRKRA, PACT, RAX, HSD-14, HSD14, Protein kinase, interferon-inducible double stranded RNA dependent activator, DYT16.

Product # :

PKA-058

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PRKRA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.8kDa.PRKRA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PRKRA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Protein Kinase IFN Double Stranded RNA Activator, also known as PRKRA, mediates the effects of interferon when a viral infection takes place. PRKRA activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA) and leads to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Mutations in PRKRA are associated with dystonia.
Synonyms
Interferon-inducible double-stranded RNA-dependent protein kinase activator A, Protein Kinase IFN Double Stranded RNA Activator, PKR-associated protein X, PKR-associating protein X, Protein activator of the interferon-induced protein kinase, Protein kinase, interferon-inducible double-stranded RNA-dependent activator, PRKRA, PACT, RAX, HSD-14, HSD14, Protein kinase, interferon-inducible double stranded RNA dependent activator, DYT16.
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 MGSMSQSRHR AEAPPLERED SGTFSLGKMI TAKPGKTPIQ VLHEYGMKTK NIPVYECERS DVQIHVPTFT FRVTVGDITC TGEGTSKKLA KHRAAEAAIN ILKANASICF AVPDPLMPDP SKQPKNQLNP IGSLQELAIH HGWRLPEYTL SQEGGPAHKR EYTTICRLES FMETGKGASK KQAKRNAAEK FLAKFSNISP ENHISLTNVV GHSLGCTWHS LRNSPGEKIN LLKRSLLSIP NTDYIQLLSE IAKEQGFNIT YLDIDELSAN GQYQCLAELS TSPITVCHGS GISCGNAQSD AAHNALQYLK IIAERK.

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:

Complement Factor D Human

Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.

Product # :

PRO-2699

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.

Source

Human Plasma.

Formulation

CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.
Synonyms
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
Physical Appearance
Sterile filtered solution.
Stability
CFD Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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:

Macrophage-Colony Stimulating Factor Mouse Recombinant

CSF-1, Lanimostim, MCSF, M-CSF.

Product # :

CYT-439

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x10⁵ units/mg.

More Info

Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

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:

Prolactin Soluble Receptor Human Recombinant

PRL-R, hPRLrI.

Product # :

CYT-595

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Extra Cellular Domain Prolactin Receptor Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containsing 210 amino acids and having a molecular mass of 23.97 kDa. The Prolactin Receptor is purified by proprietary chromatographic techniques according to Bignon et al. (1994) JBC 269; 3318-24 and tested according to Gertler et al. (1996) JBC 271; 24482-91.

Source

Escherichia Coli.

Formulation

The Prolactin Receptor was lyophilized from a concentrated (0.4mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
(c) Gel filtration at pH 8 under non denaturative conditions.

Biological Activity

Activity is determined by the dose-dependant inhibition of Prolactin stimuled proliferation of Nb2 cells and by high affinity binding of ovine Prolactin and other lactogenic hormones in 1:1 molar ratio.

More Info

Introduction
Prolactin is a pituitary hormone that plays a role in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The primary step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. Prolactin is a hormone involved in a range of significant functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. Prolactin exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane Prolactin receptor. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
Synonyms
PRL-R, hPRLrI.
Physical Appearance
Sterile filtered white lyophilized powder.
Stability
Lyophilized PRL-R although stable at room temperature for 1-2 weeks, should be stored desiccated below -18°C or preferably even at -80°C to prevent dimer formation. Upon reconstitution PRL-R should be stored sterile at 4°C between 2-7 days and for future use below -18°C. For long term storage at 4°C it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles as they cause oligomerization of the protein.
Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 18M-cm H2O not less than 100µg/ml and not more than 1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCH
FGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYL
WIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVR
CKPDHGYWSAWSPATFIQIPSDFTMNDTTVW.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 2.63 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 (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:

Protein Arginine Methyltransferase 3 Human Recombinant

Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

Product # :

ENZ-848

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PRMT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 554 amino acids (1-531 a.a) and having a molecular mass of 62.3kDa.PRMT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PRMT3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol, 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
PRMT3, also known as protein arginine N-methyltransferase 3, is a member of the protein arginine methyltransferase family. PRMT3 catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. PRMT3 operates on 40S ribosomal protein S2 ,rpS2, which is the major in-vivo substrate, additionally PRMT3 is also involved in the proper maturation of the 80S ribosome.
Synonyms
Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.
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 MGSMCSLASG ATGGRGAVEN EEDLPELSDS GDEAAWEDED DADLPHGKQQ TPCLFCNRLF TSAEETFSHC KSEHQFNIDS MVHKHGLEFY GYIKLINFIR LKNPTVEYMN SIYNPVPWEK EEYLKPVLED DLLLQFDVED LYEPVSVPFS YPNGLSENTS VVEKLKHMEA RALSAEAALA RAREDLQKMK QFAQDFVMHT DVRTCSSSTS VIADLQEDED GVYFSSYGHY GIHEEMLKDK IRTESYRDFI YQNPHIFKDK VVLDVGCGTG ILSMFAAKAG AKKVLGVDQS EILYQAMDII RLNKLEDTIT LIKGKIEEVH LPVEKVDVII SEWMGYFLLF ESMLDSVLYA KNKYLAKGGS VYPDICTISL VAVSDVNKHA DRIAFWDDVY GFKMSCMKKA VIPEAVVEVL DPKTLISEPC GIKHIDCHTT SISDLEFSSD FTLKITRTSM CTAIAGYFDI YFEKNCHNRV VFSTGPQSTK THWKQTVFLL EKPFSVKAGE ALKGKVTVHK NKKDPRSLTV TLTLNNSTQT YGLQ

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:

Prolactin Mouse Recombinant

Mammotropin, Luterotropic hormone, Lutetropin, PRL.

Product # :

CYT-321

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Prolactin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.5 kDa. The Prolactin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.

Purity

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

Biological Activity

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Leu-Pro-Ile-Cys-Ser.

More Info

Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Synonyms
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin 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-Leu-Pro-Ile-Cys.

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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation